Journal articles: 'Plasma membrane signaling'

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Wang, Nan, Marijke De Bock, Elke Decrock, Mélissa Bol, Ashish Gadicherla, Mathieu Vinken, Vera Rogiers, Feliksas F. Bukauskas, Geert Bultynck, and Luc Leybaert. "Paracrine signaling through plasma membrane hemichannels." Biochimica et Biophysica Acta (BBA) - Biomembranes 1828, no. 1 (January 2013): 35–50. http://dx.doi.org/10.1016/j.bbamem.2012.07.002.

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Chavan, Tanmay Sanjeev, Serena Muratcioglu, Richard Marszalek, Hyunbum Jang, Ozlem Keskin, Attila Gursoy, Ruth Nussinov, and Vadim Gaponenko. "Plasma membrane regulates Ras signaling networks." Cellular Logistics 5, no. 4 (October 2, 2015): e1136374. http://dx.doi.org/10.1080/21592799.2015.1136374.

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Grecco, Hernán E., Malte Schmick, and Philippe I. H. Bastiaens. "Signaling from the Living Plasma Membrane." Cell 144, no. 6 (March 2011): 897–909. http://dx.doi.org/10.1016/j.cell.2011.01.029.

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Fröhlich, Florian, Karen Moreira, Pablo S. Aguilar, Nina C. Hubner, Matthias Mann, Peter Walter, and Tobias C. Walther. "A genome-wide screen for genes affecting eisosomes reveals Nce102 function in sphingolipid signaling." Journal of Cell Biology 185, no. 7 (June 29, 2009): 1227–42. http://dx.doi.org/10.1083/jcb.200811081.

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The protein and lipid composition of eukaryotic plasma membranes is highly dynamic and regulated according to need. The sphingolipid-responsive Pkh kinases are candidates for mediating parts of this regulation, as they affect a diverse set of plasma membrane functions, such as cortical actin patch organization, efficient endocytosis, and eisosome assembly. Eisosomes are large protein complexes underlying the plasma membrane and help to sort a group of membrane proteins into distinct domains. In this study, we identify Nce102 in a genome-wide screen for genes involved in eisosome organization and Pkh kinase signaling. Nce102 accumulates in membrane domains at eisosomes where Pkh kinases also localize. The relative abundance of Nce102 in these domains compared with the rest of the plasma membrane is dynamically regulated by sphingolipids. Furthermore, Nce102 inhibits Pkh kinase signaling and is required for plasma membrane organization. Therefore, Nce102 might act as a sensor of sphingolipids that regulates plasma membrane function.

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Foley, John F. "Revealing the plasma membrane in GPCR signaling." Science Signaling 13, no. 636 (June 16, 2020): eabd3019. http://dx.doi.org/10.1126/scisignal.abd3019.

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Corre, Isabelle, Colin Niaudet, and Francois Paris. "Plasma membrane signaling induced by ionizing radiation." Mutation Research/Reviews in Mutation Research 704, no. 1-3 (April 2010): 61–67. http://dx.doi.org/10.1016/j.mrrev.2010.01.014.

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Baird, Barbara. "Plasma Membrane Heterogeneity and Receptor Mediated Signaling." Biophysical Journal 98, no. 3 (January 2010): 2a. http://dx.doi.org/10.1016/j.bpj.2009.12.007.

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Abbas, Wasim, and Georges Herbein. "Plasma membrane signaling in HIV-1 infection." Biochimica et Biophysica Acta (BBA) - Biomembranes 1838, no. 4 (April 2014): 1132–42. http://dx.doi.org/10.1016/j.bbamem.2013.06.020.

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Wills, Rachel C., and Gerald R. V. Hammond. "PI(4,5)P2: signaling the plasma membrane." Biochemical Journal 479, no. 21 (November 11, 2022): 2311–25. http://dx.doi.org/10.1042/bcj20220445.

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In the almost 70 years since the first hints of its existence, the phosphoinositide, phosphatidyl-D-myo-inositol 4,5-bisphosphate has been found to be central in the biological regulation of plasma membrane (PM) function. Here, we provide an overview of the signaling, transport and structural roles the lipid plays at the cell surface in animal cells. These include being substrate for second messenger generation, direct modulation of receptors, control of membrane traffic, regulation of ion channels and transporters, and modulation of the cytoskeleton and cell polarity. We conclude by re-evaluating PI(4,5)P2’s designation as a signaling molecule, instead proposing a cofactor role, enabling PM-selective function for many proteins.

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Ande, Sudharsana Rao, and Suresh Mishra. "Palmitoylation of prohibitin at cysteine 69 facilitates its membrane translocation and interaction with Eps 15 homology domain protein 2 (EHD2)." Biochemistry and Cell Biology 88, no. 3 (June 2010): 553–58. http://dx.doi.org/10.1139/o09-177.

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Plasma membrane translocation of specific cytosolic proteins plays an important role in cell signaling pathways. We have recently shown that prohibitin (PHB) , a protein present in the plasma membranes of various cell types, interacts with Eps 15 homology domain protein 2 (EHD2), a lipid raft protein. However, the mechanism involved in membrane translocation of PHB is not known.We report that PHB undergoes palmitoylation at cysteine 69 (Cys69), and that this palmitoylation is required for PHB's membrane translocation. Furthermore, we demonstrate that membrane translocation of PHB facilitates tyrosine phosphorylation and its interaction with EHD2. Thus, the palmitoylation and membrane translocation of PHB and its interaction with EHD2 may play a role in cell signaling.

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Ray, Supriyo, Adam Kassan, Anna R. Busija, Padmini Rangamani, and Hemal H. Patel. "The plasma membrane as a capacitor for energy and metabolism." American Journal of Physiology-Cell Physiology 310, no. 3 (February 1, 2016): C181—C192. http://dx.doi.org/10.1152/ajpcell.00087.2015.

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When considering which components of the cell are the most critical to function and physiology, we naturally focus on the nucleus, the mitochondria that regulate energy and apoptotic signaling, or other organelles such as the endoplasmic reticulum, Golgi, ribosomes, etc. Few people will suggest that the membrane is the most critical element of a cell in terms of function and physiology. Those that consider the membrane critical will point to its obvious barrier function regulated by the lipid bilayer and numerous ion channels that regulate homeostatic gradients. What becomes evident upon closer inspection is that not all membranes are created equal and that there are lipid-rich microdomains that serve as platforms of signaling and a means of communication with the intracellular environment. In this review, we explore the evolution of membranes, focus on lipid-rich microdomains, and advance the novel concept that membranes serve as “capacitors for energy and metabolism.” Within this framework, the membrane then is the primary and critical regulator of stress and disease adaptation of the cell.

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Schreiber, Rainer, Jiraporn Ousingsawat, and Karl Kunzelmann. "Targeting of Intracellular TMEM16 Proteins to the Plasma Membrane and Activation by Purinergic Signaling." International Journal of Molecular Sciences 21, no. 11 (June 5, 2020): 4065. http://dx.doi.org/10.3390/ijms21114065.

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Anoctamins such as TMEM16A and TMEM16B are Ca2+-dependent Cl− channels activated through purinergic receptor signaling. TMEM16A (ANO1), TMEM16B (ANO2) and TMEM16F (ANO6) are predominantly expressed at the plasma membrane and are therefore well accessible for functional studies. While TMEM16A and TMEM16B form halide-selective ion channels, TMEM16F and probably TMEM16E operate as phospholipid scramblases and nonselective ion channels. Other TMEM16 paralogs are expressed mainly in intracellular compartments and are therefore difficult to study at the functional level. Here, we report that TMEM16E (ANO5), -H (ANO8), -J (ANO9) and K (ANO10) are targeted to the plasma membrane when fused to a C-terminal CAAX (cysteine, two aliphatic amino acids plus methionin, serine, alanin, cystein or glutamin) motif. These paralogs produce Ca2+-dependent ion channels. Surprisingly, expression of the TMEM16 paralogs in the plasma membrane did not produce additional scramblase activity. In contrast, endogenous scrambling induced by stimulation of purinergic P2X7 receptors was attenuated, in parallel with reduced plasma membrane blebbing. This could suggest that intracellular TMEM16 paralogs operate differently when compared to plasma membrane-localized TMEM16F, and may even stabilize intracellular membranes. Alternatively, CAAX tagging, which leads to expression in non-raft compartments of the plasma membrane, may antagonize phosphatidylserine exposure by endogenous raft-located TMEM16F. CAAX-containing constructs may be useful to further investigate the molecular properties of intracellular TMEM16 proteins.

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Numrich, Johannes, and Christian Ungermann. "Endocytic Rabs in membrane trafficking and signaling." Biological Chemistry 395, no. 3 (March 1, 2014): 327–33. http://dx.doi.org/10.1515/hsz-2013-0258.

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Abstract The endolysosomal system controls the trafficking of proteins between the plasma membrane and the degradative environment of the lysosome. The early endosomal Rab5 and the late endosomal Rab7 GTPases have a key role in the transport along the endocytic pathway by recruiting tethering factors such as the hexameric CORVET and HOPS complexes that promote membrane fusion. Both Rabs are also involved in signaling at endosomal membranes and linked to amino acid sensing and autophagy, indicating that their role in trafficking may be connected to signal transduction and adaptation during cell stress. Here, we will summarize the current knowledge on the role of both Rab GTPases on both processes and discuss the possible crosstalk between them.

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Zhou, Y., C. O. Wong, K. j. Cho, D. van der Hoeven, H. Liang, D. P. Thakur, J. Luo, et al. "Membrane potential modulates plasma membrane phospholipid dynamics and K-Ras signaling." Science 349, no. 6250 (August 20, 2015): 873–76. http://dx.doi.org/10.1126/science.aaa5619.

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Grant, Michael P., Ann Stepanchick, and Gerda E. Breitwieser. "Calcium Signaling Regulates Trafficking of Familial Hypocalciuric Hypercalcemia (FHH) Mutants of the Calcium Sensing Receptor." Molecular Endocrinology 26, no. 12 (December 1, 2012): 2081–91. http://dx.doi.org/10.1210/me.2012-1232.

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Abstract Calcium-sensing receptors (CaSRs) regulate systemic Ca2+ homeostasis. Loss-of-function mutations cause familial benign hypocalciuric hypercalcemia (FHH) or neonatal severe hyperparathyroidism (NSHPT). FHH/NSHPT mutations can reduce trafficking of CaSRs to the plasma membrane. CaSR signaling is potentiated by agonist-driven anterograde CaSR trafficking, leading to a new steady state level of plasma membrane CaSR, which is maintained, with minimal functional desensitization, as long as extracellular Ca2+ is elevated. This requirement for CaSR signaling to drive CaSR trafficking to the plasma membrane led us to reconsider the mechanism(s) contributing to dysregulated trafficking of FHH/NSHPT mutants. We simultaneously monitored dynamic changes in plasma membrane levels of CaSR and intracellular Ca2+, using a chimeric CaSR construct, which allowed explicit tracking of plasma membrane levels of mutant or wild-type CaSRs in the presence of nonchimeric partners. Expression of mutants alone revealed severe defects in plasma membrane targeting and Ca2+ signaling, which were substantially rescued by coexpression with wild-type CaSR. Biasing toward heterodimerization of wild-type and FHH/NSHPT mutants revealed that intracellular Ca2+ oscillations were insufficient to rescue plasma membrane targeting. Coexpression of the nonfunctional mutant E297K with the truncation CaSRΔ868 robustly rescued trafficking and Ca2+ signaling, whereas coexpression of distinct FHH/NSHPT mutants rescued neither trafficking nor signaling. Our study suggests that rescue of FHH/NSHPT mutants requires a steady state intracellular Ca2+ response when extracellular Ca2+ is elevated and argues that Ca2+ signaling by wild-type CaSRs rescues FHH mutant trafficking to the plasma membrane.

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Saltiel, Alan R., and Jeffrey E. Pessin. "Insulin Signaling in Microdomains of the Plasma Membrane." Traffic 4, no. 11 (September 2003): 711–16. http://dx.doi.org/10.1034/j.1600-0854.2003.00119.x.

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Eckardt, Nancy A. "Sugar Signaling between Plastids and the Plasma Membrane." Plant Cell 18, no. 5 (May 2006): 1109. http://dx.doi.org/10.1105/tpc.106.180510.

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Shimizu, Yoji. "The choreography of signaling at the plasma membrane." Immunology Today 21, no. 9 (September 2000): 413. http://dx.doi.org/10.1016/s0167-5699(00)01702-3.

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Plowman, S. J., and J. F. Hancock. "Ras signaling from plasma membrane and endomembrane microdomains." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1746, no. 3 (December 2005): 274–83. http://dx.doi.org/10.1016/j.bbamcr.2005.06.004.

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Hu, Ping, and Bing-Hao Luo. "Integrin bi-directional signaling across the plasma membrane." Journal of Cellular Physiology 228, no. 2 (October 25, 2012): 306–12. http://dx.doi.org/10.1002/jcp.24154.

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Nair, Raji R., Amritanjali Kiran, and Deepak Kumar Saini. "G protein Signaling, Journeys Beyond the Plasma Membrane." Journal of the Indian Institute of Science 97, no. 1 (February 28, 2017): 95–108. http://dx.doi.org/10.1007/s41745-016-0012-2.

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Barbieri, Elisa, Pier Paolo Di Fiore, and Sara Sigismund. "Endocytic control of signaling at the plasma membrane." Current Opinion in Cell Biology 39 (April 2016): 21–27. http://dx.doi.org/10.1016/j.ceb.2016.01.012.

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Roy, Sandrine, Bruce Wyse, and John F. Hancock. "H-Ras Signaling and K-Ras Signaling Are Differentially Dependent on Endocytosis." Molecular and Cellular Biology 22, no. 14 (July 15, 2002): 5128–40. http://dx.doi.org/10.1128/mcb.22.14.5128-5140.2002.

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ABSTRACT Endocytosis is required for efficient mitogen-activated protein kinase (MAPK) activation by activated growth factor receptors. We examined if H-Ras and K-Ras proteins, which are distributed across different plasma membrane microdomains, have equal access to the endocytic compartment and whether this access is necessary for downstream signaling. Inhibition of endocytosis by dominant interfering dynamin-K44A blocked H-Ras but not K-Ras-mediated PC12 cell differentiation and selectively inhibited H-Ras- but not K-Ras-mediated Raf-1 activation in BHK cells. H-Ras- but not K-Ras-mediated Raf-1 activation was also selectively dependent on phosphoinositide 3-kinase activity. Stimulation of endocytosis and endocytic recycling by wild-type Rab5 potentiated H-Ras-mediated Raf-1 activation. In contrast, Rab5-Q79L, which stimulates endocytosis but not endocytic recycling, redistributed activated H-Ras from the plasma membrane into enlarged endosomes and inhibited H-Ras-mediated Raf-1 activation. Rab5-Q79L expression did not cause the accumulation of wild-type H-Ras in enlarged endosomes. Expression of wild-type Rab5 or Rab5-Q79L increased the specific activity of K-Ras-activated Raf-1 but did not result in any redistribution of K-Ras from the plasma membrane to endosomes. These results show that H-Ras but not K-Ras signaling though the Raf/MEK/MAPK cascade requires endocytosis and endocytic recycling. The data also suggest a mechanism for returning Raf-1 to the cytosol after plasma membrane recruitment.

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Torres, Manuel, Catalina Ana Rosselló, Paula Fernández-García, Victoria Lladó, Or Kakhlon, and Pablo Vicente Escribá. "The Implications for Cells of the Lipid Switches Driven by Protein–Membrane Interactions and the Development of Membrane Lipid Therapy." International Journal of Molecular Sciences 21, no. 7 (March 27, 2020): 2322. http://dx.doi.org/10.3390/ijms21072322.

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The cell membrane contains a variety of receptors that interact with signaling molecules. However, agonist–receptor interactions not always activate a signaling cascade. Amphitropic membrane proteins are required for signal propagation upon ligand-induced receptor activation. These proteins localize to the plasma membrane or internal compartments; however, they are only activated by ligand-receptor complexes when both come into physical contact in membranes. These interactions enable signal propagation. Thus, signals may not propagate into the cell if peripheral proteins do not co-localize with receptors even in the presence of messengers. As the translocation of an amphitropic protein greatly depends on the membrane’s lipid composition, regulation of the lipid bilayer emerges as a novel therapeutic strategy. Some of the signals controlled by proteins non-permanently bound to membranes produce dramatic changes in the cell’s physiology. Indeed, changes in membrane lipids induce translocation of dozens of peripheral signaling proteins from or to the plasma membrane, which controls how cells behave. We called these changes “lipid switches”, as they alter the cell’s status (e.g., proliferation, differentiation, death, etc.) in response to the modulation of membrane lipids. Indeed, this discovery enables therapeutic interventions that modify the bilayer’s lipids, an approach known as membrane-lipid therapy (MLT) or melitherapy.

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Nordzieke, Daniela, and Iria Medraño-Fernandez. "The Plasma Membrane: A Platform for Intra- and Intercellular Redox Signaling." Antioxidants 7, no. 11 (November 20, 2018): 168. http://dx.doi.org/10.3390/antiox7110168.

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Membranes are of outmost importance to allow for specific signal transduction due to their ability to localize, amplify, and direct signals. However, due to the double-edged nature of reactive oxygen species (ROS)—toxic at high concentrations but essential signal molecules—subcellular localization of ROS-producing systems to the plasma membrane has been traditionally regarded as a protective strategy to defend cells from unwanted side-effects. Nevertheless, specialized regions, such as lipid rafts and caveolae, house and regulate the activated/inhibited states of important ROS-producing systems and concentrate redox targets, demonstrating that plasma membrane functions may go beyond acting as a securing lipid barrier. This is nicely evinced by nicotinamide adenine dinucleotide phosphate (NADPH)-oxidases (NOX), enzymes whose primary function is to generate ROS and which have been shown to reside in specific lipid compartments. In addition, membrane-inserted bidirectional H2O2-transporters modulate their conductance precisely during the passage of the molecules through the lipid bilayer, ensuring time-scaled delivery of the signal. This review aims to summarize current evidence supporting the role of the plasma membrane as an organizing center that serves as a platform for redox signal transmission, particularly NOX-driven, providing specificity at the same time that limits undesirable oxidative damage in case of malfunction. As an example of malfunction, we explore several pathological situations in which an inflammatory component is present, such as inflammatory bowel disease and neurodegenerative disorders, to illustrate how dysregulation of plasma-membrane-localized redox signaling impacts normal cell physiology.

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Huang, Shaohui, Larry M. Lifshitz, Christine Jones, Karl D. Bellve, Clive Standley, Sonya Fonseca, Silvia Corvera, Kevin E. Fogarty, and Michael P. Czech. "Insulin Stimulates Membrane Fusion and GLUT4 Accumulation in Clathrin Coats on Adipocyte Plasma Membranes." Molecular and Cellular Biology 27, no. 9 (March 5, 2007): 3456–69. http://dx.doi.org/10.1128/mcb.01719-06.

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ABSTRACT Total internal reflection fluorescence (TIRF) microscopy reveals highly mobile structures containing enhanced green fluorescent protein-tagged glucose transporter 4 (GLUT4) within a zone about 100 nm beneath the plasma membrane of 3T3-L1 adipocytes. We developed a computer program (Fusion Assistant) that enables direct analysis of the docking/fusion kinetics of hundreds of exocytic fusion events. Insulin stimulation increases the fusion frequency of exocytic GLUT4 vesicles by ∼4-fold, increasing GLUT4 content in the plasma membrane. Remarkably, insulin signaling modulates the kinetics of the fusion process, decreasing the vesicle tethering/docking duration prior to membrane fusion. In contrast, the kinetics of GLUT4 molecules spreading out in the plasma membrane from exocytic fusion sites is unchanged by insulin. As GLUT4 accumulates in the plasma membrane, it is also immobilized in punctate structures on the cell surface. A previous report suggested these structures are exocytic fusion sites (Lizunov et al., J. Cell Biol. 169:481-489, 2005). However, two-color TIRF microscopy using fluorescent proteins fused to clathrin light chain or GLUT4 reveals these structures are clathrin-coated patches. Taken together, these data show that insulin signaling accelerates the transition from docking of GLUT4-containing vesicles to their fusion with the plasma membrane and promotes GLUT4 accumulation in clathrin-based endocytic structures on the plasma membrane.

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Quintana, Ariel, Vangipurapu Rajanikanth, Suzette Farber-Katz, Aparna Gudlur, Chen Zhang, Ji Jing, Yubin Zhou, Anjana Rao, and Patrick G. Hogan. "TMEM110 regulates the maintenance and remodeling of mammalian ER–plasma membrane junctions competent for STIM–ORAI signaling." Proceedings of the National Academy of Sciences 112, no. 51 (December 7, 2015): E7083—E7092. http://dx.doi.org/10.1073/pnas.1521924112.

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The stromal interaction molecule (STIM)–ORAI calcium release-activated calcium modulator (ORAI) pathway controls store-dependent calcium entry, a major mechanism of physiological calcium signaling in mammalian cells. The core elements of the pathway are the regulatory protein STIM1, located in the endoplasmic reticulum (ER) membrane, the calcium channel ORAI1 in the plasma membrane, and sites of close contact between the ER and the plasma membrane that permit the two proteins to interact. Research on calcium signaling has centered on STIM1, ORAI1, and a few proteins that directly modulate STIM–ORAI function. However, little is known about proteins that organize ER–plasma membrane junctions for STIM–ORAI-dependent calcium signaling. Here, we report that an ER-resident membrane protein identified in a previous genome-wide RNAi screen, transmembrane protein 110 (TMEM110), regulates the long-term maintenance of ER–plasma membrane junctions and the short-term physiological remodeling of the junctions during store-dependent calcium signaling.

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Blazer-Yost, Bonnie L., Judith C. Vahle, Jason M. Byars, and Robert L. Bacallao. "Real-time three-dimensional imaging of lipid signal transduction: apical membrane insertion of epithelial Na+ channels." American Journal of Physiology-Cell Physiology 287, no. 6 (December 2004): C1569—C1576. http://dx.doi.org/10.1152/ajpcell.00226.2004.

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In the distal tubule, Na+ resorption is mediated by epithelial Na+ channels (ENaC). Hormones such as aldosterone, vasopressin, and insulin modulate ENaC membrane targeting, assembly, and/or kinetic activity, thereby regulating salt and water homeostasis. Insulin binds to a receptor on the basal membrane to initiate a signal transduction cascade that rapidly results in an increase in apical membrane ENaC. Current models of this signaling pathway envision diffusion of signaling intermediates from the basal to the apical membrane. This necessitates diffusion of several high-molecular-weight signaling elements across a three-dimensional space. Transduction of the insulin signal involves the phosphoinositide pathway, but how and where this lipid-based signaling pathway controls ENaC activity is not known. We used tagged channels, biosensor lipid probes, and intravital imaging to investigate the role of lipids in insulin-stimulated Na+ flux. Insulin-stimulated delivery of intracellular ENaC to apical membranes was concurrent with plasma membrane-limited changes in lipid composition. Notably, in response to insulin, phosphatidylinositol 3,4,5-trisphosphate (PIP3) formed in the basolateral membrane, rapidly diffused within the bilayer, and crossed the tight junction to enter the apical membrane. This novel signaling pathway takes advantage of the fact that the lipids of the plasma membrane's inner leaflet are not constrained by the tight junction. Therefore, diffusion of PIP3 as a signal transduction intermediate occurs within a planar surface, thus facilitating swift responses and confining and controlling the signaling pathway.

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Lee, Jisoo, Yoon-Jung Kim, La-Mee Choi, Keimin Lee, Hee-Kyung Park, and Se-Young Choi. "Muscarinic Receptors and BK Channels Are Affected by Lipid Raft Disruption of Salivary Gland Cells." International Journal of Molecular Sciences 22, no. 9 (April 30, 2021): 4780. http://dx.doi.org/10.3390/ijms22094780.

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Activity-dependent fluid secretion is the most important physiological function of salivary glands and is regulated via muscarinic receptor signaling. Lipid rafts are important for G-protein coupled receptor (GPCR) signaling and ion channels in plasma membranes. However, it is not well understood whether lipid raft disruption affects all membrane events or only specific functions in muscarinic receptor-mediated water secretion in salivary gland cells. We investigated the effects of lipid raft disruption on the major membrane events of muscarinic transcellular water movement in human salivary gland (HSG) cells. We found that incubation with methyl-β-cyclodextrin (MβCD), which depletes lipid rafts, inhibited muscarinic receptor-mediated Ca2+ signaling in HSG cells and isolated mouse submandibular acinar cells. However, MβCD did not inhibit a Ca2+ increase induced by thapsigargin, which activates store-operated Ca2+ entry (SOCE). Interestingly, MβCD increased the activity of the large-conductance Ca2+-activated K+ channel (BK channel). Finally, we found that MβCD did not directly affect the translocation of aquaporin-5 (AQP5) into the plasma membrane. Our results suggest that lipid rafts maintain muscarinic Ca2+ signaling at the receptor level without directly affecting the activation of SOCE induced by intracellular Ca2+ pool depletion or the translocation of AQP5 into the plasma membrane.

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Oancea, Elena, Mary N. Teruel, Andrew F. G. Quest, and Tobias Meyer. "Green Fluorescent Protein (GFP)-tagged Cysteine-rich Domains from Protein Kinase C as Fluorescent Indicators for Diacylglycerol Signaling in Living Cells." Journal of Cell Biology 140, no. 3 (February 9, 1998): 485–98. http://dx.doi.org/10.1083/jcb.140.3.485.

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Cysteine-rich domains (Cys-domains) are ∼50–amino acid–long protein domains that complex two zinc ions and include a consensus sequence with six cysteine and two histidine residues. In vitro studies have shown that Cys-domains from several protein kinase C (PKC) isoforms and a number of other signaling proteins bind lipid membranes in the presence of diacylglycerol or phorbol ester. Here we examine the second messenger functions of diacylglycerol in living cells by monitoring the membrane translocation of the green fluorescent protein (GFP)-tagged first Cys-domain of PKC-γ (Cys1–GFP). Strikingly, stimulation of G-protein or tyrosine kinase–coupled receptors induced a transient translocation of cytosolic Cys1–GFP to the plasma membrane. The plasma membrane translocation was mimicked by addition of the diacylglycerol analogue DiC8 or the phorbol ester, phorbol myristate acetate (PMA). Photobleaching recovery studies showed that PMA nearly immobilized Cys1–GFP in the membrane, whereas DiC8 left Cys1–GFP diffusible within the membrane. Addition of a smaller and more hydrophilic phorbol ester, phorbol dibuterate (PDBu), localized Cys1–GFP preferentially to the plasma and nuclear membranes. This selective membrane localization was lost in the presence of arachidonic acid. GFP-tagged Cys1Cys2-domains and full-length PKC-γ also translocated from the cytosol to the plasma membrane in response to receptor or PMA stimuli, whereas significant plasma membrane translocation of Cys2–GFP was only observed in response to PMA addition. These studies introduce GFP-tagged Cys-domains as fluorescent diacylglycerol indicators and show that in living cells the individual Cys-domains can trigger a diacylglycerol or phorbol ester–mediated translocation of proteins to selective lipid membranes.

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Jin, Hui, J. Michael McCaffery, and Eric Grote. "Ergosterol promotes pheromone signaling and plasma membrane fusion in mating yeast." Journal of Cell Biology 180, no. 4 (February 25, 2008): 813–26. http://dx.doi.org/10.1083/jcb.200705076.

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Ergosterol depletion independently inhibits two aspects of yeast mating: pheromone signaling and plasma membrane fusion. In signaling, ergosterol participates in the recruitment of Ste5 to a polarized site on the plasma membrane. Ergosterol is thought to form microdomains within the membrane by interacting with the long acyl chains of sphingolipids. We find that although sphingolipid-free ergosterol is concentrated at sites of cell–cell contact, transmission of the pheromone signal at contact sites depends on a balanced ratio of ergosterol to sphingolipids. If a mating pair forms between ergosterol-depleted cells despite the attenuated pheromone response, the subsequent process of membrane fusion is retarded. Prm1 also participates in membrane fusion. However, ergosterol and Prm1 have independent functions and only prm1 mutant mating pairs are susceptible to contact-dependent lysis. In contrast to signaling, plasma membrane fusion is relatively insensitive to sphingolipid depletion. Thus, the sphingolipid-free pool of ergosterol promotes plasma membrane fusion.

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Harder, Thomas, and Marina Kuhn. "Selective Accumulation of Raft-Associated Membrane Protein Lat in T Cell Receptor Signaling Assemblies." Journal of Cell Biology 151, no. 2 (October 16, 2000): 199–208. http://dx.doi.org/10.1083/jcb.151.2.199.

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Activation of T cell antigen receptor (TCR) induces tyrosine phosphorylations that mediate the assembly of signaling protein complexes. Moreover, cholesterol-sphingolipid raft membrane domains have been implicated to play a role in TCR signal transduction. Here, we studied the assembly of TCR with signal transduction proteins and raft markers in plasma membrane subdomains of Jurkat T leukemic cells. We employed a novel method to immunoisolate plasma membrane subfragments that were highly concentrated in activated TCR–CD3 complexes and associated signaling proteins. We found that the raft transmembrane protein linker for activation of T cells (LAT), but not a palmitoylation-deficient non-raft LAT mutant, strongly accumulated in TCR-enriched immunoisolates in a tyrosine phosphorylation–dependent manner. In contrast, other raft-associated molecules, including protein tyrosine kinases Lck and Fyn, GM1, and cholesterol, were not highly concentrated in TCR-enriched plasma membrane immunoisolates. Many downstream signaling proteins coisolated with the TCR/LAT-enriched plasma membrane fragments, suggesting that LAT/TCR assemblies form a structural scaffold for TCR signal transduction proteins. Our results indicate that TCR signaling assemblies in plasma membrane subdomains, rather than generally concentrating raft-associated membrane proteins and lipids, form by a selective protein-mediated anchoring of the raft membrane protein LAT in vicinity of TCR.

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Dindia, Laura, Erin Faught, Zoya Leonenko, Raymond Thomas, and Mathilakath M. Vijayan. "Rapid cortisol signaling in response to acute stress involves changes in plasma membrane order in rainbow trout liver." American Journal of Physiology-Endocrinology and Metabolism 304, no. 11 (June 1, 2013): E1157—E1166. http://dx.doi.org/10.1152/ajpendo.00500.2012.

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The activation of genomic signaling in response to stressor-mediated cortisol elevation has been studied extensively in teleosts. However, very little is known about the rapid signaling events elicited by this steroid. We tested the hypothesis that cortisol modulates key stress-related signaling pathways in response to an acute stressor in fish liver. To this end, we investigated the effect of an acute stressor on biophysical properties of plasma membrane and on stressor-related protein phosphorylation in rainbow trout ( Oncorhynchus mykiss) liver. A role for cortisol in modulating the acute cellular stress response was ascertained by blocking the stressor-induced elevation of this steroid by metyrapone. The acute stressor exposure increased plasma cortisol levels and liver membrane fluidity (measured by anisotropy of 1,6-diphenyl-1,3,5-hexatriene), but these responses were abolished by metyrapone. Atomic force microscopy further confirmed biophysical alterations in liver plasma membrane in response to stress, including changes in membrane domain topography. The changes in membrane order did not correspond to any changes in membrane fatty acid components after stress, suggesting that changes in membrane structure may be associated with cortisol incorporation into the lipid bilayer. Plasma cortisol elevation poststress correlated positively with activation of intracellular stress signaling pathways, including increased phosphorylation of extracellular signal-related kinases as well as several putative PKA and PKC but not Akt substrate proteins. Together, our results indicate that stressor-induced elevation of plasma cortisol level is associated with alterations in plasma membrane fluidity and rapid activation of stress-related signaling pathways in trout liver.

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Hancock, John F., Robert G. Parton, Dan Nicolau, Sarah Plowman, Tianhai Tian, and Angus Harding. "S1e1-2 Plasma membrane signaling platforms(S1-e1: "Unraveling the membrane microdomains using new biophysical tools",Symposia,Abstract,Meeting Program of EABS & BSJ 2006)." Seibutsu Butsuri 46, supplement2 (2006): S108. http://dx.doi.org/10.2142/biophys.46.s108_3.

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Sehgal, Pravin B. "Plasma membrane rafts and chaperones in cytokine/STAT signaling." Acta Biochimica Polonica 50, no. 3 (September 30, 2003): 583–94. http://dx.doi.org/10.18388/abp.2003_3652.

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We and others have recently obtained data suggesting that cytokine-STAT signaling in many different cell-types is a chaperoned pathway initiated at the level of specialized plasma membrane microdomains called "rafts" (the "raft-STAT signaling hypothesis"). These findings are of broad significance in that all cytokines and growth factors initiate signaling in target cells by interacting with respective cell-surface receptors. The new data suggest that raft microdomains represent the units of function at the cell-surface through which ligand-stimulated STAT signaling is initiated. Moreover, recent evidence shows the involvement of chaperone proteins in regulating the STAT signaling pathway. These chaperones include the human homolog of the tumorous imaginal disc 1 protein (hTid1) which associates with Janus kinase 2 (JAK2) at the level of the plasma membrane, heat shock protein 90 (HSP90) which associates with STAT3 and STAT1 proteins in caveolin-1-containing raft and cytoplasmic complexes, and glucose regulated protein 58 (GRP58/ER-60/ERp57), a thiol dependent protein-disulfide isomerase, found in association with STAT3 "statosome" complexes in the cytosol and in the raft fraction. We suggest a function of the HSP90 chaperone system in preserving IL-6/STAT3 signaling in liver cells in the context of fever. The identification and function of protein partners associated with specific STAT species in rafts and in cytosolic complexes, and in the efficient departure of cytokine-activated STATs from the cytosolic face of rafts towards the cell nucleus are now areas of active investigation.

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Foley, John F. "MAPping PI3K signaling to endosomes." Science Signaling 13, no. 658 (November 17, 2020): eabf7090. http://dx.doi.org/10.1126/scisignal.abf7090.

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Antón, Olga, Alicia Batista, Jaime Millán, Laura Andrés-Delgado, Rosa Puertollano, Isabel Correas, and Miguel A. Alonso. "An essential role for the MAL protein in targeting Lck to the plasma membrane of human T lymphocytes." Journal of Experimental Medicine 205, no. 13 (December 8, 2008): 3201–13. http://dx.doi.org/10.1084/jem.20080552.

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The MAL protein is an essential component of the specialized machinery for apical targeting in epithelial cells. The src family kinase Lck plays a pivotal role in T cell signaling. We show that MAL is required in T cells for efficient expression of Lck at the plasma membrane and activation of IL-2 transcription. To investigate the mechanism by which MAL regulates Lck targeting, we analyzed the dynamics of Lck and found that it travels to the plasma membrane in specific transport carriers containing MAL. Coimmunoprecipitation experiments indicated an association of MAL with Lck. Both carrier formation and partitioning of Lck into detergent-insoluble membranes were ablated in the absence of MAL. Polarization of T cell receptor for antigen (TCR) and microtubule-organizing center to immunological synapse (IS) were also defective. Although partial correction of the latter defects was possible by forced expression of Lck at the plasma membrane, their complete correction, formation of transport vesicles, partitioning of Lck, and restoration of signaling pathways, which are required for IL-2 transcription up-regulation, were achieved by exogenous expression of MAL. We concluded that MAL is required for recruitment of Lck to specialized membranes and formation of specific transport carriers for Lck targeting. This novel transport pathway is crucial for TCR-mediated signaling and IS assembly.

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Trotter, Kevin W., Iain D. C. Fraser, Gregory K. Scott, M. Jackson Stutts, John D. Scott, and Sharon L. Milgram. "Alternative Splicing Regulates the Subcellular Localization of a-Kinase Anchoring Protein 18 Isoforms." Journal of Cell Biology 147, no. 7 (December 27, 1999): 1481–92. http://dx.doi.org/10.1083/jcb.147.7.1481.

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The cAMP-dependent protein kinase (PKA) is localized to specific subcellular compartments by association with A-kinase anchoring proteins (AKAPs). AKAPs are a family of functionally related proteins that bind the regulatory (R) subunit of PKA with high affinity and target the kinase to specific subcellular organelles. Recently, AKAP18, a low molecular weight plasma membrane AKAP that facilitates PKA-mediated phosphorylation of the L-type Ca2+ channel, was cloned. We now report the cloning of two additional isoforms of AKAP18, which we have designated AKAP18β and AKAP18γ, that arise from alternative mRNA splicing. The AKAP18 isoforms share a common R subunit binding site, but have distinct targeting domains. The original AKAP18 (renamed AKAP18α) and AKAP18β target the plasma membrane when expressed in HEK-293 cells, while AKAP18γ is cytosolic. When expressed in epithelial cells, AKAP18α is targeted to lateral membranes, whereas AKAP18β is accumulated at the apical membrane. A 23-amino acid insert, following the plasma membrane targeting domain, facilitates the association of AKAP18β with the apical membrane. The data suggest that AKAP18 isoforms are differentially targeted to modulate distinct intracellular signaling events. Furthermore, the data suggest that plasma membrane AKAPs may be targeted to subdomains of the cell surface, adding additional specificity in intracellular signaling.

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Aminin, Dmitry, and Peter Illes. "Purinergic Signaling in Neuroinflammation." International Journal of Molecular Sciences 22, no. 23 (November 29, 2021): 12895. http://dx.doi.org/10.3390/ijms222312895.

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ATP is stored in millimolar concentrations within the intracellular medium but may be released to extracellular sites either through the damaged plasma membrane or by means of various transporters [...]

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Ferraro, Jeffrey T., Mani Daneshmand, Rena Bizios, and Victor Rizzo. "Depletion of plasma membrane cholesterol dampens hydrostatic pressure and shear stress-induced mechanotransduction pathways in osteoblast cultures." American Journal of Physiology-Cell Physiology 286, no. 4 (April 2004): C831—C839. http://dx.doi.org/10.1152/ajpcell.00224.2003.

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The preferential association of cholesterol and sphingolipids within plasma membranes forms organized compartments termed lipid rafts. Addition of caveolin proteins to this lipid milieu induces the formation of specialized invaginated plasma membrane structures called caveolae. Both lipid rafts and caveolae are purported to function in vesicular transport and cell signaling. We and others have shown that disassembly of rafts and caveolae through depletion of plasma membrane cholesterol mitigates mechanotransduction processes in endothelial cells. Because osteoblasts are subjected to fluid-mechanical forces, we hypothesize that cholesterol-rich plasma membrane microdomains also serve the mechanotransduction process in this cell type. Cultured human fetal osteoblasts were subjected to either sustained hydrostatic pressure or laminar shear stress using a pressure column or parallel-plate apparatus, respectively. We found that sustained hydrostatic pressure induced protein tyrosine phosphorylation, activation of extracellular signal-regulated kinase (ERK)1/2, and enhanced expression of c- fos in both time- and magnitude-dependent manners. Similar responses were observed in cells subjected to laminar shear stress. Both sustained hydrostatic pressure- and shear stress-induced signaling were significantly reduced in osteoblasts pre-exposed to either filipin or methyl-β-cyclodextrin. These mechanotransduction responses were restored on reconstitution of lipid rafts and caveolae, which suggests that cholesterol-rich plasma membrane microdomains participate in the mechanotransduction process in osteoblasts. In addition, mechanical force-induced phosphoproteins were localized within caveolin-containing membranes. These data support the concept that lipid rafts and caveolae serve a general function as cell surface mechanotransduction sites within the plasma membrane.

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Son, Aran, Seonghee Park, Dong Min Shin, and Shmuel Muallem. "Orai1 and STIM1 in ER/PM junctions: roles in pancreatic cell function and dysfunction." American Journal of Physiology-Cell Physiology 310, no. 6 (March 15, 2016): C414—C422. http://dx.doi.org/10.1152/ajpcell.00349.2015.

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Membrane contact sites (MCS) are critical junctions that form between the endoplasmic reticulum (ER) and membranes of various organelles, including the plasma membrane (PM). Signaling complexes, including mediators of Ca2+signaling, are assembled within MCS, such as the ER/PM junction. This is most evident in polarized epithelial cells, such as pancreatic cells. Core Ca2+signaling proteins cluster at the apical pole, the site of inositol 1,4,5-trisphosphate-mediated Ca2+release and Orai1/transient receptor potential canonical-mediated store-dependent Ca2+entry. Recent advances have characterized the proteins that tether the membranes at MCS and the role of these proteins in modulating physiological and pathological intracellular signaling. This review discusses recent advances in the characterization of Ca2+signaling at ER/PM junctions and the relation of these junctions to physiological and pathological Ca2+signaling in pancreatic acini.

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Li, Fang-Yi, Zhen-Feng Zhang, Stephanie Voss, Yao-Wen Wu, Yu-Fen Zhao, Yan-Mei Li, and Yong-Xiang Chen. "Inhibition of K-Ras4B-plasma membrane association with a membrane microdomain-targeting peptide." Chemical Science 11, no. 3 (2020): 826–32. http://dx.doi.org/10.1039/c9sc04726c.

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Mithöfer, Axel, Jürgen Ebel, and Hubert H. Felle. "Cation Fluxes Cause Plasma Membrane Depolarization Involved in β-Glucan Elicitor-Signaling in Soybean Roots." Molecular Plant-Microbe Interactions® 18, no. 9 (September 2005): 983–90. http://dx.doi.org/10.1094/mpmi-18-0983.

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Inducible and specific ion fluxes on plasma membranes represent very early events during elicitation of plant cells. The hierarchy of such ion fluxes involved is still unknown. The effect of Phytophthora sojae-derived β-glucan elicitors on the plasma membrane potential as well as on surface K+, Ca2+, and H+ fluxes has been investigated on soybean roots using ion-selective microelectrodes. β-Glucans with different degrees of polymerization transiently depolarized the plasma membrane. The elicitor concentration necessary for half-maximal depolarization closely resembled the corresponding binding affinities of soybean root membranes toward the respective β-glucans. Upon repeated elicitor treatment, the root cells responded partially refractory, suggesting a complex responsiveness of the system. Within the root hair space, characteristic decreasing K+- and Ca2+-free concentrations were induced by the elicitors, probably causing depolarization through the influx of positive charges. Whereas K+ fluxes were inverted after passing the K+ equilibrium (Nernst-) potential, Ca2+ influx continued. No anion fluxes sufficient to account for charge compensation were observed under the same experimental conditions. K+ and Ca2+ fluxes as well as depolarization were inhibited by 100 μM or less of the Ca2+ antagonist La3+. Contrasting other systems, in soybean the main cause for elicitor-induced plasma membrane depolarization is the activation of cation instead of anion fluxes.

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Lajoie, Patrick, Emily A. Partridge, Ginette Guay, Jacky G. Goetz, Judy Pawling, Annick Lagana, Bharat Joshi, James W. Dennis, and Ivan R. Nabi. "Plasma membrane domain organization regulates EGFR signaling in tumor cells." Journal of Cell Biology 179, no. 2 (October 15, 2007): 341–56. http://dx.doi.org/10.1083/jcb.200611106.

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Macromolecular complexes exhibit reduced diffusion in biological membranes; however, the physiological consequences of this characteristic of plasma membrane domain organization remain elusive. We report that competition between the galectin lattice and oligomerized caveolin-1 microdomains for epidermal growth factor (EGF) receptor (EGFR) recruitment regulates EGFR signaling in tumor cells. In mammary tumor cells deficient for Golgi β1,6N-acetylglucosaminyltransferase V (Mgat5), a reduction in EGFR binding to the galectin lattice allows an increased association with stable caveolin-1 cell surface microdomains that suppresses EGFR signaling. Depletion of caveolin-1 enhances EGFR diffusion, responsiveness to EGF, and relieves Mgat5 deficiency–imposed restrictions on tumor cell growth. In Mgat5+/+ tumor cells, EGFR association with the galectin lattice reduces first-order EGFR diffusion rates and promotes receptor interaction with the actin cytoskeleton. Importantly, EGFR association with the lattice opposes sequestration by caveolin-1, overriding its negative regulation of EGFR diffusion and signaling. Therefore, caveolin-1 is a conditional tumor suppressor whose loss is advantageous when β1,6GlcNAc-branched N-glycans are below a threshold for optimal galectin lattice formation.

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Saarikangas, Juha, Hongxia Zhao, and Pekka Lappalainen. "Regulation of the Actin Cytoskeleton-Plasma Membrane Interplay by Phosphoinositides." Physiological Reviews 90, no. 1 (January 2010): 259–89. http://dx.doi.org/10.1152/physrev.00036.2009.

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The plasma membrane and the underlying cortical actin cytoskeleton undergo continuous dynamic interplay that is responsible for many essential aspects of cell physiology. Polymerization of actin filaments against cellular membranes provides the force for a number of cellular processes such as migration, morphogenesis, and endocytosis. Plasma membrane phosphoinositides (especially phosphatidylinositol bis- and trisphosphates) play a central role in regulating the organization and dynamics of the actin cytoskeleton by acting as platforms for protein recruitment, by triggering signaling cascades, and by directly regulating the activities of actin-binding proteins. Furthermore, a number of actin-associated proteins, such as BAR domain proteins, are capable of directly deforming phosphoinositide-rich membranes to induce plasma membrane protrusions or invaginations. Recent studies have also provided evidence that the actin cytoskeleton-plasma membrane interactions are misregulated in a number of pathological conditions such as cancer and during pathogen invasion. Here, we summarize the wealth of knowledge on how the cortical actin cytoskeleton is regulated by phosphoinositides during various cell biological processes. We also discuss the mechanisms by which interplay between actin dynamics and certain membrane deforming proteins regulate the morphology of the plasma membrane.

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Iwasaki, Yukimoto, Takafumi Itoh, Yusuke Hagi, Sakura Matsuta, Aki Nishiyama, Genki Chaya, Yuki Kobayashi, Kotaro Miura, and Setsuko Komatsu. "Proteomics Analysis of Plasma Membrane Fractions of the Root, Leaf, and Flower of Rice." International Journal of Molecular Sciences 21, no. 19 (September 23, 2020): 6988. http://dx.doi.org/10.3390/ijms21196988.

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The plasma membrane regulates biological processes such as ion transport, signal transduction, endocytosis, and cell differentiation/proliferation. To understand the functional characteristics and organ specificity of plasma membranes, plasma membrane protein fractions from rice root, etiolated leaf, green leaf, developing leaf sheath, and flower were analyzed by proteomics. Among the proteins identified, 511 were commonly accumulated in the five organs, whereas 270, 132, 359, 146, and 149 proteins were specifically accumulated in the root, etiolated leaf, green leaf, developing leaf sheath, and developing flower, respectively. The principle component analysis revealed that the functions of the plasma membrane in the root was different from those of green and etiolated leaves and that the plasma membrane protein composition of the leaf sheath was similar to that of the flower, but not that of the green leaf. Functional classification revealed that the root plasma membrane has more transport-related proteins than the leaf plasma membrane. Furthermore, the leaf sheath and flower plasma membranes were found to be richer in proteins involved in signaling and cell function than the green leaf plasma membrane. To validate the proteomics data, immunoblot analysis was carried out, focusing on four heterotrimeric G protein subunits, Gα, Gβ, Gγ1, and Gγ2. All subunits could be detected by both methods and, in particular, Gγ1 and Gγ2 required concentration by immunoprecipitation for mass spectrometry detection.

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Medina-Puche, Laura, and Rosa Lozano-Durán. "Plasma membrane-to-organelle communication in plant stress signaling." Current Opinion in Plant Biology 69 (October 2022): 102269. http://dx.doi.org/10.1016/j.pbi.2022.102269.

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Wu, Xiaomo, Liqiang Weng, Jinyan Zhang, Xiaolong Liu, and Jianqing Huang. "The Plasma Membrane Calcium ATPases in Calcium Signaling Network." Current Protein & Peptide Science 19, no. 8 (June 13, 2018): 813–22. http://dx.doi.org/10.2174/1389203719666180416122745.

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Irani, Niloufer G., Simone Di Rubbo, Evelien Mylle, Jos Van den Begin, Joanna Schneider-Pizoń, Jaroslava Hniliková, Miroslav Šíša, et al. "Fluorescent castasterone reveals BRI1 signaling from the plasma membrane." Nature Chemical Biology 8, no. 6 (May 6, 2012): 583–89. http://dx.doi.org/10.1038/nchembio.958.

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Harding, Angus S., and John F. Hancock. "Using plasma membrane nanoclusters to build better signaling circuits." Trends in Cell Biology 18, no. 8 (August 2008): 364–71. http://dx.doi.org/10.1016/j.tcb.2008.05.006.

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Journal articles on the topic 'Plasma membrane signaling'

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