Bibliographies thématiques / Microdomain compartmentalization

Littérature scientifique sur le sujet « Microdomain compartmentalization »

Auteur : Grafiati

Publié le 11 mars 2023

Créez une référence correcte selon les styles APA, MLA, Chicago, Harvard et plusieurs autres

Choisissez une source :

Sommaire

Articles de revues
Thèses
Chapitres de livres

Consultez les listes thématiques d’articles de revues, de livres, de thèses, de rapports de conférences et d’autres sources académiques sur le sujet « Microdomain compartmentalization ».

À côté de chaque source dans la liste de références il y a un bouton « Ajouter à la bibliographie ». Cliquez sur ce bouton, et nous générerons automatiquement la référence bibliographique pour la source choisie selon votre style de citation préféré : APA, MLA, Harvard, Vancouver, Chicago, etc.

Vous pouvez aussi télécharger le texte intégral de la publication scolaire au format pdf et consulter son résumé en ligne lorsque ces informations sont inclues dans les métadonnées.

Articles de revues sur le sujet "Microdomain compartmentalization"

Watson, Robert T., Satoshi Shigematsu, Shian-Huey Chiang, Silvia Mora, Makoto Kanzaki, Ian G. Macara, Alan R. Saltiel et Jeffrey E. Pessin. « Lipid raft microdomain compartmentalization of TC10 is required for insulin signaling and GLUT4 translocation ». Journal of Cell Biology 154, n^o 4 (13 août 2001) : 829–40. http://dx.doi.org/10.1083/jcb.200102078.

Texte intégral

Résumé :

Recent studies indicate that insulin stimulation of glucose transporter (GLUT)4 translocation requires at least two distinct insulin receptor–mediated signals: one leading to the activation of phosphatidylinositol 3 (PI-3) kinase and the other to the activation of the small GTP binding protein TC10. We now demonstrate that TC10 is processed through the secretory membrane trafficking system and localizes to caveolin-enriched lipid raft microdomains. Although insulin activated the wild-type TC10 protein and a TC10/H-Ras chimera that were targeted to lipid raft microdomains, it was unable to activate a TC10/K-Ras chimera that was directed to the nonlipid raft domains. Similarly, only the lipid raft–localized TC10/ H-Ras chimera inhibited GLUT4 translocation, whereas the TC10/K-Ras chimera showed no significant inhibitory activity. Furthermore, disruption of lipid raft microdomains by expression of a dominant-interfering caveolin 3 mutant (Cav3/DGV) inhibited the insulin stimulation of GLUT4 translocation and TC10 lipid raft localization and activation without affecting PI-3 kinase signaling. These data demonstrate that the insulin stimulation of GLUT4 translocation in adipocytes requires the spatial separation and distinct compartmentalization of the PI-3 kinase and TC10 signaling pathways.

Styles APA, Harvard, Vancouver, ISO, etc.

Collin, Guillaume, Mélanie Franco, Valérie Simon, Christine Bénistant et Serge Roche. « The Tom1L1-Clathrin Heavy Chain Complex Regulates Membrane Partitioning of the Tyrosine Kinase Src Required for Mitogenic and Transforming Activities ». Molecular and Cellular Biology 27, n^o 21 (4 septembre 2007) : 7631–40. http://dx.doi.org/10.1128/mcb.00543-07.

Texte intégral

Résumé :

ABSTRACT Compartmentalization of Src tyrosine kinases (SFK) plays an important role in signal transduction induced by a number of extracellular stimuli. For example, Src mitogenic signaling induced by platelet-derived growth factor (PDGF) is initiated in cholesterol-enriched microdomain caveolae. How this Src subcellular localization is regulated is largely unknown. Here we show that the Tom1L1-clathrin heavy chain (CHC) complex negatively regulates the level of SFK in caveolae needed for the induction of DNA synthesis. Tom1L1 is both an interactor and a substrate of SFK. Intriguingly, it stimulates Src activity without promoting mitogenic signaling. We found that, upon association with CHC, Tom1L1 reduced the level of SFK in caveolae, thereby preventing its association with the PDGF receptor, which is required for the induction of mitogenesis. Similarly, the Tom1L1-CHC complex reduced also the level of oncogenic Src in cholesterol-enriched microdomains, thus affecting both its capacity to induce DNA synthesis and cell transformation. Conversely, Tom1L1, when not associated with CHC, accumulated in caveolae and promoted Src-driven DNA synthesis. We concluded that the Tom1L1-CHC complex defines a novel mechanism involved in negative regulation of mitogenic and transforming signals, by modulating SFK partitioning at the plasma membrane.

Styles APA, Harvard, Vancouver, ISO, etc.

Terrin, Anna, Stefania Monterisi, Alessandra Stangherlin, Anna Zoccarato, Andreas Koschinski, Nicoletta C. Surdo, Marco Mongillo et al. « PKA and PDE4D3 anchoring to AKAP9 provides distinct regulation of cAMP signals at the centrosome ». Journal of Cell Biology 198, n^o 4 (20 août 2012) : 607–21. http://dx.doi.org/10.1083/jcb.201201059.

Texte intégral

Résumé :

Previous work has shown that the protein kinase A (PKA)–regulated phosphodiesterase (PDE) 4D3 binds to A kinase–anchoring proteins (AKAPs). One such protein, AKAP9, localizes to the centrosome. In this paper, we investigate whether a PKA–PDE4D3–AKAP9 complex can generate spatial compartmentalization of cyclic adenosine monophosphate (cAMP) signaling at the centrosome. Real-time imaging of fluorescence resonance energy transfer reporters shows that centrosomal PDE4D3 modulated a dynamic microdomain within which cAMP concentration selectively changed over the cell cycle. AKAP9-anchored, centrosomal PKA showed a reduced activation threshold as a consequence of increased autophosphorylation of its regulatory subunit at S114. Finally, disruption of the centrosomal cAMP microdomain by local displacement of PDE4D3 impaired cell cycle progression as a result of accumulation of cells in prophase. Our findings describe a novel mechanism of PKA activity regulation that relies on binding to AKAPs and consequent modulation of the enzyme activation threshold rather than on overall changes in cAMP levels. Further, we provide for the first time direct evidence that control of cell cycle progression relies on unique regulation of centrosomal cAMP/PKA signals.

Styles APA, Harvard, Vancouver, ISO, etc.

Hong, Dihui, Dov Jaron, Donald G. Buerk et Kenneth A. Barbee. « Transport-dependent calcium signaling in spatially segregated cellular caveolar domains ». American Journal of Physiology-Cell Physiology 294, n^o 3 (mars 2008) : C856—C866. http://dx.doi.org/10.1152/ajpcell.00278.2007.

Texte intégral

Résumé :

We developed a two-dimensional model of transport-dependent intracellular calcium signaling in endothelial cells (ECs). Our purpose was to evaluate the effects of spatial colocalization of endothelial nitric oxide synthase (eNOS) and capacitative calcium entry (CCE) channels in caveolae on eNOS activation in response to ATP. Caveolae are specialized microdomains of the plasma membrane that contain a variety of signaling molecules to optimize their interactions and regulate their activity. In ECs, these molecules include CCE channels and eNOS. To achieve a quantitative understanding of the mechanisms of microdomain calcium signaling and the preferential sensitivity of eNOS to calcium entering the cell through CCE channels, we constructed a mathematical model incorporating the cell morphology and cellular physiological processes. The model predicts that the spatial segregation of calcium channels in ECs can create transport-dependent sharp gradients in calcium concentration within the cell. The calcium concentration gradient is affected by channel density and cell geometry. This transport-dependent calcium signaling specificity effect is enhanced in ECs by increasing the spatial segregation of the caveolar signaling domains. Our simulation significantly advances the understanding of how Ca2+, despite its many potential actions, can mediate selective activation of signaling pathways. We show that diffusion-limited calcium transport allows functional compartmentalization of signaling pathways based on the spatial arrangements of Ca2+ sources and targets.

Styles APA, Harvard, Vancouver, ISO, etc.

Frolikova, Michaela, Eliska Valaskova, Jiri Cerny, Audrey Lumeau, Natasa Sebkova, Veronika Palenikova, Noemi Sanches-Hernandez, Alzbeta Pohlova, Pavla Manaskova-Postlerova et Katerina Dvorakova-Hortova. « Addressing the Compartmentalization of Specific Integrin Heterodimers in Mouse Sperm ». International Journal of Molecular Sciences 20, n^o 5 (26 février 2019) : 1004. http://dx.doi.org/10.3390/ijms20051004.

Texte intégral

Résumé :

Integrins are transmembrane cell receptors involved in two crucial mechanisms for successful fertilization, namely, mammalian intracellular signaling and cell adhesion. Integrins α6β4, α3β1 and α6β1 are three major laminin receptors expressed on the surface of mammalian cells including gametes, and the presence of individual integrin subunits α3, α6, β1 and β4 has been previously detected in mammalian sperm. However, to date, proof of the existence of individual heterodimer pairs in sperm and their detailed localization is missing. The major conclusion of this study is evidence that the β4 integrin subunit is expressed in mouse sperm and that it pairs with subunit α6; additionally, there is a detailed identification of integrin heterodimer pairs across individual membranes in an intact mouse sperm head. We also demonstrate the existence of β4 integrin mRNAs in round spermatids and spermatogonia by q-RT-PCR, which was further supported by sequencing the PCR products. Using super-resolution microscopy accompanied by colocalization analysis, we located integrin subunits as follows: α6/β4-inner apical acrosomal membrane and equatorial segment; α3, α6/β1, β4-plasma membrane overlaying the apical acrosome; and α3/β1-outer acrosomal membrane. The existence of α6β4, α3β1 and α6β1 heterodimers was further confirmed by proximity ligation assay (PLA). In conclusion, we delivered detailed characterization of α3, α6, β1 and β4 integrin subunits, showing their presence in distinct compartments of the intact mouse sperm head. Moreover, we identified sperm-specific localization for heterodimers α6β4, α3β1 and α6β1, and their membrane compartmentalization and the presented data show a complexity of membranes overlaying specialized microdomain structures in the sperm head. Their different protein compositions of these individual membrane rafts may play a specialized role, based on their involvement in sperm-epithelium and sperm-egg interaction.

Styles APA, Harvard, Vancouver, ISO, etc.

Aota, Hiroyuki, Yotaro Morishima et Mikiharu Kamachi. « COMPARTMENTALIZATION OF ZINQII) TETRAPHENYLPORPHYRIN IN A HYDROPHOBIC MICRODOMAIN OF AN AMPHIPHILIC POLYELECTROLYTE : A PHYSICOCHEMICAL MODEL OF BIOLOGICAL METALLOPORPHYRIN SYSTEMS ». Photochemistry and Photobiology 57, s1 (mai 1993) : 989–95. http://dx.doi.org/10.1111/j.1751-1097.1993.tb02960.x.

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

Marchetti, Marta, Marie-Noelle Monier, Alexandre Fradagrada, Keith Mitchell, Florence Baychelier, Pierre Eid, Ludger Johannes et Christophe Lamaze. « Stat-mediated Signaling Induced by Type I and Type II Interferons (IFNs) Is Differentially Controlled through Lipid Microdomain Association and Clathrin-dependent Endocytosis of IFN Receptors ». Molecular Biology of the Cell 17, n^o 7 (juillet 2006) : 2896–909. http://dx.doi.org/10.1091/mbc.e06-01-0076.

Texte intégral

Résumé :

Type I (α/β) and type II (γ) interferons (IFNs) bind to distinct receptors, although they activate the same signal transducer and activator of transcription, Stat1, raising the question of how signal specificity is maintained. Here, we have characterized the sorting of IFN receptors (IFN-Rs) at the plasma membrane and the role it plays in IFN-dependent signaling and biological activities. We show that both IFN-α and IFN-γ receptors are internalized by a classical clathrin- and dynamin-dependent endocytic pathway. Although inhibition of clathrin-dependent endocytosis blocked the uptake of IFN-α and IFN-γ receptors, this inhibition only affected IFN-α–induced Stat1 and Stat2 signaling. Furthermore, the antiviral and antiproliferative activities induced by IFN-α but not IFN-γ were also affected. Finally, we show that, unlike IFN-α receptors, activated IFN-γ receptors rapidly become enriched in plasma membrane lipid microdomains. We conclude that IFN-R compartmentalization at the plasma membrane, through clathrin-dependent endocytosis and lipid-based microdomains, plays a critical role in the signaling and biological responses induced by IFNs and contributes to establishing specificity within the Jak/Stat signaling pathway.

Styles APA, Harvard, Vancouver, ISO, etc.

Bavari, Sina, Catharine M. Bosio, Elizabeth Wiegand, Gordon Ruthel, Amy B. Will, Thomas W. Geisbert, Michael Hevey, Connie Schmaljohn, Alan Schmaljohn et M. Javad Aman. « Lipid Raft Microdomains ». Journal of Experimental Medicine 195, n^o 5 (4 mars 2002) : 593–602. http://dx.doi.org/10.1084/jem.20011500.

Texte intégral

Résumé :

Spatiotemporal aspects of filovirus entry and release are poorly understood. Lipid rafts act as functional platforms for multiple cellular signaling and trafficking processes. Here, we report the compartmentalization of Ebola and Marburg viral proteins within lipid rafts during viral assembly and budding. Filoviruses released from infected cells incorporated raft-associated molecules, suggesting that viral exit occurs at the rafts. Ectopic expression of Ebola matrix protein and glycoprotein supported raft-dependent release of filamentous, virus-like particles (VLPs), strikingly similar to live virus as revealed by electron microscopy. Our findings also revealed that the entry of filoviruses requires functional rafts, identifying rafts as the site of virus attack. The identification of rafts as the gateway for the entry and exit of filoviruses and raft-dependent generation of VLPs have important implications for development of therapeutics and vaccination strategies against infections with Ebola and Marburg viruses.

Styles APA, Harvard, Vancouver, ISO, etc.

Grisan, Francesca, Liliana F. Iannucci, Nicoletta C. Surdo, Andrea Gerbino, Sofia Zanin, Giulietta Di Benedetto, Tullio Pozzan et Konstantinos Lefkimmiatis. « PKA compartmentalization links cAMP signaling and autophagy ». Cell Death & ; Differentiation 28, n^o 8 (19 mars 2021) : 2436–49. http://dx.doi.org/10.1038/s41418-021-00761-8.

Texte intégral

Résumé :

AbstractAutophagy is a highly regulated degradative process crucial for maintaining cell homeostasis. This important catabolic mechanism can be nonspecific, but usually occurs with fine spatial selectivity (compartmentalization), engaging only specific subcellular sites. While the molecular machines driving autophagy are well understood, the involvement of localized signaling events in this process is not well defined. Among the pathways that regulate autophagy, the cyclic AMP (cAMP)/protein kinase A (PKA) cascade can be compartmentalized in distinct functional units called microdomains. However, while it is well established that, depending on the cell type, cAMP can inhibit or promote autophagy, the role of cAMP/PKA microdomains has not been tested. Here we show not only that the effects on autophagy of the same cAMP elevation differ in different cell types, but that they depend on a highly complex sub-compartmentalization of the signaling cascade. We show in addition that, in HT-29 cells, in which autophagy is modulated by cAMP rising treatments, PKA activity is strictly regulated in space and time by phosphatases, which largely prevent the phosphorylation of soluble substrates, while membrane-bound targets are less sensitive to the action of these enzymes. Interestingly, we also found that the subcellular distribution of PKA type-II regulatory PKA subunits hinders the effect of PKA on autophagy, while displacement of type-I regulatory PKA subunits has no effect. Our data demonstrate that local PKA activity can occur independently of local cAMP concentrations and provide strong evidence for a link between localized PKA signaling events and autophagy.

Styles APA, Harvard, Vancouver, ISO, etc.

Olsen, Anne S. B., et Nils J. Færgeman. « Sphingolipids : membrane microdomains in brain development, function and neurological diseases ». Open Biology 7, n^o 5 (mai 2017) : 170069. http://dx.doi.org/10.1098/rsob.170069.

Texte intégral

Résumé :

Sphingolipids are highly enriched in the nervous system where they are pivotal constituents of the plasma membranes and are important for proper brain development and functions. Sphingolipids are not merely structural elements, but are also recognized as regulators of cellular events by their ability to form microdomains in the plasma membrane. The significance of such compartmentalization spans broadly from being involved in differentiation of neurons and synaptic transmission to neuronal–glial interactions and myelin stability. Thus, perturbations of the sphingolipid metabolism can lead to rearrangements in the plasma membrane, which has been linked to the development of various neurological diseases. Studying microdomains and their functions has for a long time been synonymous with studying the role of cholesterol. However, it is becoming increasingly clear that microdomains are very heterogeneous, which among others can be ascribed to the vast number of sphingolipids. In this review, we discuss the importance of microdomains with emphasis on sphingolipids in brain development and function as well as how disruption of the sphingolipid metabolism (and hence microdomains) contributes to the pathogenesis of several neurological diseases.

Styles APA, Harvard, Vancouver, ISO, etc.

Plus de sources

Thèses sur le sujet "Microdomain compartmentalization"

Balycheva, Marina. « Microdomain–specific localization of functional L-type calcium channels in atrial cardiomyocytes : novel concept of local regulation and remodelling in disease ». Doctoral thesis, 2015. http://hdl.handle.net/11562/924530.

Texte intégral

Résumé :

no
Recently, novel concept of microdomain-specific regulation in cardiac cells have greatly extended our understanding of how specific subcellular localization impacts on channel function and regulation. Microdomain is a small region of cell membrane, which has a distinct structure, composition and function. It has been recognized that discrete clusters of different ion channels exist in the sarcolemma in different microdomains such as T-tubules, caveolae. This study addresses the hypothesis that distinct spatial compartmentalization of functional calcium channels in different intercellular microdomains are coupled with structural proteins and receptors and play an important role in unique Ca2+ signaling in atrial cardiomyocytes in health and pathology. Using several technical approaches (super-resolution scanning and whole-cell patch-clamp, confocal and electron microscopy), this study aims to investigate characteristics of subcellular micrdomains such as T-tubules and caveolae in atrial cardiomyocytes; and to answer the question whether in atrial cardiomyocytes functional L-type calcium channels (LTCCs) are specifically distributed within different microdomains and forming signalling complexes with receptors, that potentially causes a unique atrial cardiomyocyte Ca2+ signaling process. First, it was found that atrial cells could be characterised by heterogeneous T-tubule system the structure of which influenced by the cell size and atrial chamber localization. This study provides the first direct evidence for two distinct subpopulations of functional LTCCs in rat and human healthy atrial cardiomyocytes, with a micro-domain-specific regulation of their biophysical properties. In atrial cells, L-type calcium channels are equally distributed inside and outside of T-tubules, in contrast to ventricular cardiomyocytes where LTCCs are clustered in T-tubules (Bhargava, Lin et al. 2013). The population of LTCCs observed outside of T-tubules was associated with caveolae. LTCCs located in caveolae contribute essentially to atrial Ca2+ signaling, particularly in cardiomyocytes lacking the organized T-tubule network. Second, β1-adreneric stimulation, which increases single LTCC activity and antiadrenergic effect of adenosine on functional LTCCs were investigated in both microdomains in rat atrial cariomyocytes. Third, using animal model, heart failure was found to be associated with loss of T-tubule structure and decrease in single amplitude of T-tubular LTCCs localized in atrial cardiomyocytes. Fourth, human studies revealed, that chronic atrial fibrillation is associated with the loss of T-tubule structure and downregulation of the L-type calcium current with increased activity of single LTCCs localized in T-tubule microdomains and the loss channels outside of T-tubules. Decrease of calcium current was associated with the downregulation of gene expression. These results support the notion that functional L-type calcium channels are linked with structural components of cardiac membrane and undergo remodelling in association with loss of structures during pathology.

Styles APA, Harvard, Vancouver, ISO, etc.

Chapitres de livres sur le sujet "Microdomain compartmentalization"

Redden, John M., Kimberly L. Dodge-Kafka et Michael S. Kapiloff. « Function to Failure : Compartmentalization of Cardiomyocyte Signaling by A-Kinase-Anchoring Proteins ». Dans Microdomains in the Cardiovascular System, 37–57. Cham : Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-54579-0_3.

Texte intégral

Styles APA, Harvard, Vancouver, ISO, etc.

Nous offrons des réductions sur tous les plans premium pour les auteurs dont les œuvres sont incluses dans des sélections littéraires thématiques. Contactez-nous pour obtenir un code promo unique!