Log in

Relevant bibliographies by topics / Vesicle tethering complex exocyst / Journal articles

To see the other types of publications on this topic, follow the link: Vesicle tethering complex exocyst.

Journal articles on the topic 'Vesicle tethering complex exocyst'

Author: Grafiati

Published: 4 June 2021

Last updated: 4 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the top 50 journal articles for your research on the topic 'Vesicle tethering complex exocyst.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.

1

Wiederkehr, Andreas, Johan-Owen De Craene, Susan Ferro-Novick, and Peter Novick. "Functional specialization within a vesicle tethering complex." Journal of Cell Biology 167, no. 5 (2004): 875–87. http://dx.doi.org/10.1083/jcb.200408001.

Full text

Abstract:

The exocyst is an octameric protein complex required to tether secretory vesicles to exocytic sites and to retain ER tubules at the apical tip of budded cells. Unlike the other five exocyst genes, SEC3, SEC5, and EXO70 are not essential for growth or secretion when either the upstream activator rab, Sec4p, or the downstream SNARE-binding component, Sec1p, are overproduced. Analysis of the suppressed sec3Δ, sec5Δ, and exo70Δ strains demonstrates that the corresponding proteins confer differential effects on vesicle targeting and ER inheritance. Sec3p and Sec5p are more critical than Exo70p for

APA, Harvard, Vancouver, ISO, and other styles

2

Luo, Guangzuo, Jian Zhang, and Wei Guo. "The role of Sec3p in secretory vesicle targeting and exocyst complex assembly." Molecular Biology of the Cell 25, no. 23 (2014): 3813–22. http://dx.doi.org/10.1091/mbc.e14-04-0907.

Full text

Abstract:

During membrane trafficking, vesicular carriers are transported and tethered to their cognate acceptor compartments before soluble N-ethylmaleimide–sensitive factor attachment protein (SNARE)-mediated membrane fusion. The exocyst complex was believed to target and tether post-Golgi secretory vesicles to the plasma membrane during exocytosis. However, no definitive experimental evidence is available to support this notion. We developed an ectopic targeting assay in yeast in which each of the eight exocyst subunits was expressed on the surface of mitochondria. We find that most of the exocyst su

APA, Harvard, Vancouver, ISO, and other styles

3

Eckardt, Nancy A. "An Exocyst Vesicle Tethering Complex in Plants." Plant Cell 20, no. 5 (2008): 1188. http://dx.doi.org/10.1105/tpc.108.200511.

Full text

APA, Harvard, Vancouver, ISO, and other styles

4

Zhang, Weiwei, Lei Huang, Chunhua Zhang, and Christopher J. Staiger. "Arabidopsis myosin XIK interacts with the exocyst complex to facilitate vesicle tethering during exocytosis." Plant Cell 33, no. 7 (2021): 2454–78. http://dx.doi.org/10.1093/plcell/koab116.

Full text

Abstract:

Abstract Myosin motors are essential players in secretory vesicle trafficking and exocytosis in yeast and mammalian cells; however, similar roles in plants remain a matter for debate, at least for diffusely growing cells. Here, we demonstrate that Arabidopsis (Arabidopsis thaliana) myosin XIK, via its globular tail domain (GTD), participates in the vesicle tethering step of exocytosis through direct interactions with the exocyst complex. Specifically, myosin XIK GTD bound directly to several exocyst subunits in vitro and functional fluorescently tagged XIK colocalized with multiple exocyst sub

APA, Harvard, Vancouver, ISO, and other styles

5

Fendrych, Matyáš, Lukáš Synek, Tamara Pečenková, et al. "Visualization of the exocyst complex dynamics at the plasma membrane of Arabidopsis thaliana." Molecular Biology of the Cell 24, no. 4 (2013): 510–20. http://dx.doi.org/10.1091/mbc.e12-06-0492.

Full text

Abstract:

The exocyst complex, an effector of Rho and Rab GTPases, is believed to function as an exocytotic vesicle tether at the plasma membrane before soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE) complex formation. Exocyst subunits localize to secretory-active regions of the plasma membrane, exemplified by the outer domain of Arabidopsis root epidermal cells. Using variable-angle epifluorescence microscopy, we visualized the dynamics of exocyst subunits at this domain. The subunits colocalized in defined foci at the plasma membrane, distinct from endocytic sites. Exocy

APA, Harvard, Vancouver, ISO, and other styles

6

Morgera, Francesca, Margaret R. Sallah, Michelle L. Dubuke, et al. "Regulation of exocytosis by the exocyst subunit Sec6 and the SM protein Sec1." Molecular Biology of the Cell 23, no. 2 (2012): 337–46. http://dx.doi.org/10.1091/mbc.e11-08-0670.

Full text

Abstract:

Trafficking of protein and lipid cargo through the secretory pathway in eukaryotic cells is mediated by membrane-bound vesicles. Secretory vesicle targeting and fusion require a conserved multisubunit protein complex termed the exocyst, which has been implicated in specific tethering of vesicles to sites of polarized exocytosis. The exocyst is directly involved in regulating soluble N-ethylmaleimide–sensitive factor (NSF) attachment protein receptor (SNARE) complexes and membrane fusion through interactions between the Sec6 subunit and the plasma membrane SNARE protein Sec9. Here we show anoth

APA, Harvard, Vancouver, ISO, and other styles

7

Riquelme, Meritxell, Erin L. Bredeweg, Olga Callejas-Negrete, et al. "The Neurospora crassa exocyst complex tethers Spitzenkörper vesicles to the apical plasma membrane during polarized growth." Molecular Biology of the Cell 25, no. 8 (2014): 1312–26. http://dx.doi.org/10.1091/mbc.e13-06-0299.

Full text

Abstract:

Fungal hyphae are among the most highly polarized cells. Hyphal polarized growth is supported by tip-directed transport of secretory vesicles, which accumulate temporarily in a stratified manner in an apical vesicle cluster, the Spitzenkörper. The exocyst complex is required for tethering of secretory vesicles to the apical plasma membrane. We determined that the presence of an octameric exocyst complex is required for the formation of a functional Spitzenkörper and maintenance of regular hyphal growth in Neurospora crassa. Two distinct localization patterns of exocyst subunits at the hyphal t

APA, Harvard, Vancouver, ISO, and other styles

8

Medkova, Martina, Y. Ellen France, Jeff Coleman, and Peter Novick. "The rab Exchange Factor Sec2p Reversibly Associates with the Exocyst." Molecular Biology of the Cell 17, no. 6 (2006): 2757–69. http://dx.doi.org/10.1091/mbc.e05-10-0917.

Full text

Abstract:

Activation of the rab GTPase, Sec4p, by its exchange factor, Sec2p, is needed for polarized transport of secretory vesicles to exocytic sites and for exocytosis. A small region in the C-terminal half of Sec2p regulates its localization. Loss of this region results in temperature-sensitive growth and the depolarized accumulation of secretory vesicles. Here, we show that Sec2p associates with the exocyst, an octameric effector of Sec4p involved in tethering secretory vesicles to the plasma membrane. Specifically, the exocyst subunit Sec15p directly interacts with Sec2p. This interaction normally

APA, Harvard, Vancouver, ISO, and other styles

9

Lira, Matías, Rodrigo G. Mira, Francisco J. Carvajal, Pedro Zamorano, Nibaldo C. Inestrosa, and Waldo Cerpa. "Glutamatergic Receptor Trafficking and Delivery: Role of the Exocyst Complex." Cells 9, no. 11 (2020): 2402. http://dx.doi.org/10.3390/cells9112402.

Full text

Abstract:

Cells comprise several intracellular membrane compartments that allow them to function properly. One of these functions is cargo movement, typically proteins and membranes within cells. These cargoes ride microtubules through vesicles from Golgi and recycling endosomes to the plasma membrane in order to be delivered and exocytosed. In neurons, synaptic functions employ this cargo trafficking to maintain inter-neuronal communication optimally. One of the complexes that oversee vesicle trafficking and tethering is the exocyst. The exocyst is a protein complex containing eight subunits first iden

APA, Harvard, Vancouver, ISO, and other styles

10

Fais, Milena, Giovanna Sanna, Manuela Galioto, et al. "LRRK2 Modulates the Exocyst Complex Assembly by Interacting with Sec8." Cells 10, no. 2 (2021): 203. http://dx.doi.org/10.3390/cells10020203.

Full text

Abstract:

Mutations in LRRK2 play a critical role in both familial and sporadic Parkinson’s disease (PD). Up to date, the role of LRRK2 in PD onset and progression remains largely unknown. However, experimental evidence highlights a critical role of LRRK2 in the control of vesicle trafficking, likely by Rab phosphorylation, that in turn may regulate different aspects of neuronal physiology. Here we show that LRRK2 interacts with Sec8, one of eight subunits of the exocyst complex. The exocyst complex is an evolutionarily conserved multisubunit protein complex mainly involved in tethering secretory vesicl

APA, Harvard, Vancouver, ISO, and other styles

11

Novick, P., M. Medkova, G. Dong, A. Hutagalung, K. Reinisch, and B. Grosshans. "Interactions between Rabs, tethers, SNAREs and their regulators in exocytosis." Biochemical Society Transactions 34, no. 5 (2006): 683–86. http://dx.doi.org/10.1042/bst0340683.

Full text

Abstract:

Sec2p is the exchange factor that activates Sec4p, the Rab GTPase controlling the final stage of the yeast exocytic pathway. Sec2p is recruited to secretory vesicles by Ypt32-GTP, a Rab controlling exit from the Golgi. Sec15p, a subunit of the octameric exocyst tethering complex and an effector of Sec4p, binds to Sec2p on secretory vesicles, displacing Ypt32p. Sec2p mutants defective in the region 450–508 amino acids bind to Sec15p more tightly. In these mutants, Sec2p accumulates in the cytosol in a complex with the exocyst and is not recruited to vesicles by Ypt32p. Thus the region 450–508 a

APA, Harvard, Vancouver, ISO, and other styles

12

Rossi, Guendalina, Kelly Watson, Wade Kennedy, and Patrick Brennwald. "The tomosyn homologue, Sro7, is a direct effector of the Rab GTPase, Sec4, in post-Golgi vesicle tethering." Molecular Biology of the Cell 29, no. 12 (2018): 1476–86. http://dx.doi.org/10.1091/mbc.e18-02-0138.

Full text

Abstract:

The tomosyn/Sro7 family is thought to play an important role in cell surface trafficking both as an effector of Rab family GTPases and as a regulator of plasma-membrane SNARE function. Recent work has determined the binding site of GTP-bound Sec4 on Sro7. Here we examine the effect of mutations in Sro7 that block Sec4 binding in determining the role of this interaction in Sro7 function. Using an in vitro vesicle:vesicle tethering assay, we find that most of Sro7’s ability to tether vesicles is blocked by mutations that disrupt binding to Sec4-GTP. Similarly, genetic analysis demonstrates that

APA, Harvard, Vancouver, ISO, and other styles

13

Inoue, Mayumi, Shian-Huey Chiang, Louise Chang, Xiao-Wei Chen, and Alan R. Saltiel. "Compartmentalization of the Exocyst Complex in Lipid Rafts Controls Glut4 Vesicle Tethering." Molecular Biology of the Cell 17, no. 5 (2006): 2303–11. http://dx.doi.org/10.1091/mbc.e06-01-0030.

Full text

Abstract:

Lipid raft microdomains act as organizing centers for signal transduction. We report here that the exocyst complex, consisting of Exo70, Sec6, and Sec8, regulates the compartmentalization of Glut4-containing vesicles at lipid raft domains in adipocytes. Exo70 is recruited by the G protein TC10 after activation by insulin and brings with it Sec6 and Sec8. Knockdowns of these proteins block insulin-stimulated glucose uptake. Moreover, their targeting to lipid rafts is required for glucose uptake and Glut4 docking at the plasma membrane. The assembly of this complex also requires the PDZ domain p

APA, Harvard, Vancouver, ISO, and other styles

14

Prigent, Magali, Thierry Dubois, Graça Raposo, et al. "ARF6 controls post-endocytic recycling through its downstream exocyst complex effector." Journal of Cell Biology 163, no. 5 (2003): 1111–21. http://dx.doi.org/10.1083/jcb.200305029.

Full text

Abstract:

The small guanosine triphosphate (GTP)–binding protein ADP-ribosylation factor (ARF) 6 regulates membrane recycling to regions of plasma membrane remodeling via the endocytic pathway. Here, we show that GTP–bound ARF6 interacts with Sec10, a subunit of the exocyst complex involved in docking of vesicles with the plasma membrane. We found that Sec10 localization in the perinuclear region is not restricted to the trans-Golgi network, but extends to recycling endosomes. In addition, we report that depletion of Sec5 exocyst subunit or dominant inhibition of Sec10 affects the function and the morph

APA, Harvard, Vancouver, ISO, and other styles

15

Rivera-Molina, Felix, and Derek Toomre. "Live-cell imaging of exocyst links its spatiotemporal dynamics to various stages of vesicle fusion." Journal of Cell Biology 201, no. 5 (2013): 673–80. http://dx.doi.org/10.1083/jcb.201212103.

Full text

Abstract:

Tethers play ubiquitous roles in membrane trafficking and influence the specificity of vesicle attachment. Unlike soluble N-ethyl-maleimide–sensitive fusion attachment protein receptors (SNAREs), the spatiotemporal dynamics of tethers relative to vesicle fusion are poorly characterized. The most extensively studied tethering complex is the exocyst, which spatially targets vesicles to sites on the plasma membrane. By using a mammalian genetic replacement strategy, we were able to assemble fluorescently tagged Sec8 into the exocyst complex, which was shown to be functional by biochemical, traffi

APA, Harvard, Vancouver, ISO, and other styles

16

Arasaki, Kohei, Hana Kimura, Mitsuo Tagaya, and Craig R. Roy. "Legionella remodels the plasma membrane–derived vacuole by utilizing exocyst components as tethers." Journal of Cell Biology 217, no. 11 (2018): 3863–72. http://dx.doi.org/10.1083/jcb.201801208.

Full text

Abstract:

During the initial stage of infection, Legionella pneumophila secretes effectors that promote the fusion of endoplasmic reticulum (ER)–derived vesicles with the Legionella-containing vacuole (LCV). This fusion leads to a remodeling of the plasma membrane (PM)–derived LCV into a specialized ER-like compartment that supports bacterial replication. Although the effector DrrA has been shown to activate the small GTPase Rab1, it remains unclear how DrrA promotes the tethering of host vesicles with the LCV. Here, we show that Sec5, Sec15, and perhaps Sec6, which are subunits of the exocyst that func

APA, Harvard, Vancouver, ISO, and other styles

17

Liu, Jianglan, Xiaofeng Zuo, Peng Yue, and Wei Guo. "Phosphatidylinositol 4,5-Bisphosphate Mediates the Targeting of the Exocyst to the Plasma Membrane for Exocytosis in Mammalian Cells." Molecular Biology of the Cell 18, no. 11 (2007): 4483–92. http://dx.doi.org/10.1091/mbc.e07-05-0461.

Full text

Abstract:

The exocyst is an evolutionarily conserved octameric protein complex that tethers post-Golgi secretory vesicles at the plasma membrane for exocytosis. To elucidate the mechanism of vesicle tethering, it is important to understand how the exocyst physically associates with the plasma membrane (PM). In this study, we report that the mammalian exocyst subunit Exo70 associates with the PM through its direct interaction with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). Furthermore, we have identified key conserved residues at the C-terminus of Exo70 that are crucial for the interaction of Exo

APA, Harvard, Vancouver, ISO, and other styles

18

Synek, Lukáš, Roman Pleskot, Juraj Sekereš, et al. "Plasma membrane phospholipid signature recruits the plant exocyst complex via the EXO70A1 subunit." Proceedings of the National Academy of Sciences 118, no. 36 (2021): e2105287118. http://dx.doi.org/10.1073/pnas.2105287118.

Full text

Abstract:

Polarized exocytosis is essential for many vital processes in eukaryotic cells, where secretory vesicles are targeted to distinct plasma membrane domains characterized by their specific lipid–protein composition. Heterooctameric protein complex exocyst facilitates the vesicle tethering to a target membrane and is a principal cell polarity regulator in eukaryotes. The architecture and molecular details of plant exocyst and its membrane recruitment have remained elusive. Here, we show that the plant exocyst consists of two modules formed by SEC3–SEC5–SEC6–SEC8 and SEC10–SEC15–EXO70–EXO84 subunit

APA, Harvard, Vancouver, ISO, and other styles

19

Mathieson, Erin M., Yasuyuki Suda, Mark Nickas, et al. "Vesicle Docking to the Spindle Pole Body Is Necessary to Recruit the Exocyst During Membrane Formation inSaccharomyces cerevisiae." Molecular Biology of the Cell 21, no. 21 (2010): 3693–707. http://dx.doi.org/10.1091/mbc.e10-07-0563.

Full text

Abstract:

During meiosis II in Saccharomyces cerevisiae, the cytoplasmic face of the spindle pole body, referred to as the meiosis II outer plaque (MOP), is modified in both composition and structure to become the initiation site for de novo formation of a membrane called the prospore membrane. The MOP serves as a docking complex for precursor vesicles that are targeted to its surface. Using fluorescence resonance energy transfer analysis, the orientation of coiled-coil proteins within the MOP has been determined. The N-termini of two proteins, Mpc54p and Spo21p, were oriented toward the outer surface o

APA, Harvard, Vancouver, ISO, and other styles

20

Marković, Vedrana, Ivan Kulich, and Viktor Žárský. "Functional Specialization within the EXO70 Gene Family in Arabidopsis." International Journal of Molecular Sciences 22, no. 14 (2021): 7595. http://dx.doi.org/10.3390/ijms22147595.

Full text

Abstract:

Localized delivery of plasma-membrane and cell-wall components is a crucial process for plant cell growth. One of the regulators of secretory-vesicle targeting is the exocyst tethering complex. The exocyst mediates first interaction between transport vesicles and the target membrane before their fusion is performed by SNARE proteins. In land plants, genes encoding the EXO70 exocyst subunit underwent an extreme proliferation with 23 paralogs present in the Arabidopsis (Arabidopsis thaliana) genome. These paralogs often acquired specialized functions during evolution. Here, we analyzed functiona

APA, Harvard, Vancouver, ISO, and other styles

21

Sakurai-Yageta, Mika, Chiara Recchi, Gaëlle Le Dez, et al. "The interaction of IQGAP1 with the exocyst complex is required for tumor cell invasion downstream of Cdc42 and RhoA." Journal of Cell Biology 181, no. 6 (2008): 985–98. http://dx.doi.org/10.1083/jcb.200709076.

Full text

Abstract:

Invadopodia are actin-based membrane protrusions formed at contact sites between invasive tumor cells and the extracellular matrix with matrix proteolytic activity. Actin regulatory proteins participate in invadopodia formation, whereas matrix degradation requires metalloproteinases (MMPs) targeted to invadopodia. In this study, we show that the vesicle-tethering exocyst complex is required for matrix proteolysis and invasion of breast carcinoma cells. We demonstrate that the exocyst subunits Sec3 and Sec8 interact with the polarity protein IQGAP1 and that this interaction is triggered by acti

APA, Harvard, Vancouver, ISO, and other styles

22

Conibear, Elizabeth, Jessica N. Cleck, and Tom H. Stevens. "Vps51p Mediates the Association of the GARP (Vps52/53/54) Complex with the Late Golgi t-SNARE Tlg1p." Molecular Biology of the Cell 14, no. 4 (2003): 1610–23. http://dx.doi.org/10.1091/mbc.e02-10-0654.

Full text

Abstract:

Multisubunit tethering complexes may contribute to the specificity of membrane fusion events by linking transport vesicles to their target membrane in an initial recognition event that promotes SNARE assembly. However, the interactions that link tethering factors to the other components of the vesicle fusion machinery are still largely unknown. We have previously identified three subunits of a Golgi-localized complex (the Vps52/53/54 complex) that is required for retrograde transport to the late Golgi. This complex interacts with a Rab and a SNARE protein found at the late Golgi and is related

APA, Harvard, Vancouver, ISO, and other styles

23

De Craene, Johan-Owen, Jeff Coleman, Paula Estrada de Martin, et al. "Rtn1p Is Involved in Structuring the Cortical Endoplasmic Reticulum." Molecular Biology of the Cell 17, no. 7 (2006): 3009–20. http://dx.doi.org/10.1091/mbc.e06-01-0080.

Full text

Abstract:

The endoplasmic reticulum (ER) contains both cisternal and reticular elements in one contiguous structure. We identified rtn1Δ in a systematic screen for yeast mutants with altered ER morphology. The ER in rtn1Δ cells is predominantly cisternal rather than reticular, yet the net surface area of ER is not significantly changed. Rtn1-green fluorescent protein (GFP) associates with the reticular ER at the cell cortex and with the tubules that connect the cortical ER to the nuclear envelope, but not with the nuclear envelope itself. Rtn1p overexpression also results in an altered ER structure. Rtn

APA, Harvard, Vancouver, ISO, and other styles

24

VerPlank, Lynn, and Rong Li. "Cell Cycle-regulated Trafficking of Chs2 Controls Actomyosin Ring Stability during Cytokinesis." Molecular Biology of the Cell 16, no. 5 (2005): 2529–43. http://dx.doi.org/10.1091/mbc.e04-12-1090.

Full text

Abstract:

Cytokinesis requires the coordination of many cellular complexes, particularly those involved in the constriction and reconstruction of the plasma membrane in the cleavage furrow. We have investigated the regulation and function of vesicle transport and fusion during cytokinesis in budding yeast. By using time-lapse confocal microscopy, we show that post-Golgi vesicles, as well as the exocyst, a complex required for the tethering and fusion of these vesicles, localize to the bud neck at a precise time just before spindle disassembly and actomyosin ring contraction. Using mutants affecting cycl

APA, Harvard, Vancouver, ISO, and other styles

25

Luo, L., M. Hannemann, S. Koenig, et al. "The Caenorhabditis elegans GARP complex contains the conserved Vps51 subunit and is required to maintain lysosomal morphology." Molecular Biology of the Cell 22, no. 14 (2011): 2564–78. http://dx.doi.org/10.1091/mbc.e10-06-0493.

Full text

Abstract:

In yeast the Golgi-associated retrograde protein (GARP) complex is required for tethering of endosome-derived transport vesicles to the late Golgi. It consists of four subunits—Vps51p, Vps52p, Vps53p, and Vps54p—and shares similarities with other multimeric tethering complexes, such as the conserved oligomeric Golgi (COG) and the exocyst complex. Here we report the functional characterization of the GARP complex in the nematode Caenorhabditis elegans. Furthermore, we identified the C. elegans Vps51 subunit, which is conserved in all eukaryotes. GARP mutants are viable but show lysosomal defect

APA, Harvard, Vancouver, ISO, and other styles

26

Grosshans, Bianka L., Anna Andreeva, Akanksha Gangar, et al. "The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p." Journal of Cell Biology 172, no. 1 (2006): 55–66. http://dx.doi.org/10.1083/jcb.200510016.

Full text

Abstract:

Rab guanosine triphosphatases regulate intracellular membrane traffic by binding specific effector proteins. The yeast Rab Sec4p plays multiple roles in the polarized transport of post-Golgi vesicles to, and their subsequent fusion with, the plasma membrane, suggesting the involvement of several effectors. Yet, only one Sec4p effector has been documented to date: the exocyst protein Sec15p. The exocyst is an octameric protein complex required for tethering secretory vesicles, which is a prerequisite for membrane fusion. In this study, we describe the identification of a second Sec4p effector,

APA, Harvard, Vancouver, ISO, and other styles

27

Zhang, Xiaoyu, Kelly Orlando, Bing He, et al. "Membrane association and functional regulation of Sec3 by phospholipids and Cdc42." Journal of Cell Biology 180, no. 1 (2008): 145–58. http://dx.doi.org/10.1083/jcb.200704128.

Full text

Abstract:

The exocyst is an octameric protein complex implicated in tethering post-Golgi secretory vesicles at the plasma membrane in preparation for fusion. However, it is not clear how the exocyst is targeted to and physically associates with specific domains of the plasma membrane and how its functions are regulated at those regions. We demonstrate that the N terminus of the exocyst component Sec3 directly interacts with phosphatidylinositol 4,5-bisphosphate. In addition, we have identified key residues in Sec3 that are critical for its binding to the guanosine triphosphate–bound form of Cdc42. Genet

APA, Harvard, Vancouver, ISO, and other styles

28

Liu, Jianglan, Peng Yue, Vira V. Artym, Susette C. Mueller, and Wei Guo. "The Role of the Exocyst in Matrix Metalloproteinase Secretion and Actin Dynamics during Tumor Cell Invadopodia Formation." Molecular Biology of the Cell 20, no. 16 (2009): 3763–71. http://dx.doi.org/10.1091/mbc.e08-09-0967.

Full text

Abstract:

Invadopodia are actin-rich membrane protrusions formed by tumor cells that degrade the extracellular matrix for invasion. Invadopodia formation involves membrane protrusions driven by Arp2/3-mediated actin polymerization and secretion of matrix metalloproteinases (MMPs) at the focal degrading sites. The exocyst mediates the tethering of post-Golgi secretory vesicles at the plasma membrane for exocytosis and has recently been implicated in regulating actin dynamics during cell migration. Here, we report that the exocyst plays a pivotal role in invadopodial activity. With RNAi knockdown of the e

APA, Harvard, Vancouver, ISO, and other styles

29

Zajac, Allison, Xiaoli Sun, Jian Zhang, and Wei Guo. "Cyclical Regulation of the Exocyst and Cell Polarity Determinants for Polarized Cell Growth." Molecular Biology of the Cell 16, no. 3 (2005): 1500–1512. http://dx.doi.org/10.1091/mbc.e04-10-0896.

Full text

Abstract:

Polarized exocytosis is important for morphogenesis and cell growth. The exocyst is a multiprotein complex implicated in tethering secretory vesicles at specific sites of the plasma membrane for exocytosis. In the budding yeast, the exocyst is localized to sites of bud emergence or the tips of small daughter cells, where it mediates secretion and cell surface expansion. To understand how exocytosis is spatially controlled, we systematically analyzed the localization of Sec15p, a member of the exocyst complex and downstream effector of the rab protein Sec4p, in various mutants. We found that th

APA, Harvard, Vancouver, ISO, and other styles

30

Walsh, Tony G., Yong Li, Christopher M. Williams, Elizabeth W. Aitken, Robert K. Andrews, and Alastair W. Poole. "Loss of the exocyst complex component EXOC3 promotes hemostasis and accelerates arterial thrombosis." Blood Advances 5, no. 3 (2021): 674–86. http://dx.doi.org/10.1182/bloodadvances.2020002515.

Full text

Abstract:

Abstract The exocyst is an octameric complex comprising 8 distinct protein subunits, exocyst complex components (EXOC) 1 to 8. It has an established role in tethering secretory vesicles to the plasma membrane, but its relevance to platelet granule secretion and function remains to be determined. Here, EXOC3 conditional knockout (KO) mice in the megakaryocyte/platelet lineage were generated to assess exocyst function in platelets. Significant defects in platelet aggregation, integrin activation, α-granule (P-selectin and platelet factor 4), dense granule, and lysosomal granule secretion were de

APA, Harvard, Vancouver, ISO, and other styles

31

Hou, Hongna, Jianbo Fang, Jiahui Liang, et al. "OsExo70B1 Positively Regulates Disease Resistance to Magnaporthe oryzae in Rice." International Journal of Molecular Sciences 21, no. 19 (2020): 7049. http://dx.doi.org/10.3390/ijms21197049.

Full text

Abstract:

The exocyst, an evolutionarily conserved octameric protein complex, mediates tethering of vesicles to the plasma membrane in the early stage of exocytosis. Arabidopsis Exo70, a subunit of the exocyst complex, has been found to be involved in plant immunity. Here, we characterize the function of OsExo70B1 in rice. OsExo70B1 mainly expresses in leaf and shoot and its expression is induced by pathogen-associated molecular patterns (PAMPs) and rice blast fungus Magnaporthe oryzae (M. oryzae). Knocking out OsExo70B1 results in significantly decreased resistance and defense responses to M. oryzae co

APA, Harvard, Vancouver, ISO, and other styles

32

Žárský, Viktor, and Martin Potocký. "Recycling domains in plant cell morphogenesis: small GTPase effectors, plasma membrane signalling and the exocyst." Biochemical Society Transactions 38, no. 2 (2010): 723–28. http://dx.doi.org/10.1042/bst0380723.

Full text

Abstract:

The Rho/Rop small GTPase regulatory module is central for initiating exocytotically ACDs (active cortical domains) in plant cell cortex, and a growing array of Rop regulators and effectors are being discovered in plants. Structural membrane phospholipids are important constituents of cells as well as signals, and phospholipid-modifying enzymes are well known effectors of small GTPases. We have shown that PLDs (phospholipases D) and their product, PA (phosphatidic acid), belong to the regulators of the secretory pathway in plants. We have also shown that specific NOXs (NADPH oxidases) producing

APA, Harvard, Vancouver, ISO, and other styles

33

Estey, Mathew P., Caterina Di Ciano-Oliveira, Carol D. Froese, Margaret T. Bejide, and William S. Trimble. "Distinct roles of septins in cytokinesis: SEPT9 mediates midbody abscission." Journal of Cell Biology 191, no. 4 (2010): 741–49. http://dx.doi.org/10.1083/jcb.201006031.

Full text

Abstract:

Septins are a family of GTP-binding proteins implicated in mammalian cell division. Most studies examining the role of septins in this process have treated the family as a whole, thus neglecting the possibility that individual members may have diverse functions. To address this, we individually depleted each septin family member expressed in HeLa cells by siRNA and assayed for defects in cell division by immunofluorescence and time-lapse microscopy. Depletion of SEPT2, SEPT7, and SEPT11 causes defects in the early stages of cytokinesis, ultimately resulting in binucleation. In sharp contrast,

APA, Harvard, Vancouver, ISO, and other styles

34

Arasaki, Kohei, Daichi Takagi, Akiko Furuno, et al. "A new role for RINT-1 in SNARE complex assembly at the trans-Golgi network in coordination with the COG complex." Molecular Biology of the Cell 24, no. 18 (2013): 2907–17. http://dx.doi.org/10.1091/mbc.e13-01-0014.

Full text

Abstract:

Docking and fusion of transport vesicles/carriers with the target membrane involve a tethering factor–mediated initial contact followed by soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE)–catalyzed membrane fusion. The multisubunit tethering CATCHR family complexes (Dsl1, COG, exocyst, and GARP complexes) share very low sequence homology among subunits despite likely evolving from a common ancestor and participate in fundamentally different membrane trafficking pathways. Yeast Tip20, as a subunit of the Dsl1 complex, has been implicated in retrograde transport from

APA, Harvard, Vancouver, ISO, and other styles

35

Elbert, Maya, Guendalina Rossi, and Patrick Brennwald. "The Yeast Par-1 Homologs Kin1 and Kin2 Show Genetic and Physical Interactions with Components of the Exocytic Machinery." Molecular Biology of the Cell 16, no. 2 (2005): 532–49. http://dx.doi.org/10.1091/mbc.e04-07-0549.

Full text

Abstract:

Kin1 and Kin2 are Saccharomyces cerevisiae counterparts of Par-1, the Caenorhabditis elegans kinase essential for the establishment of polarity in the one cell embryo. Here, we present evidence for a novel link between Kin1, Kin2, and the secretory machinery of the budding yeast. We isolated KIN1 and KIN2 as suppressors of a mutant form of Rho3, a Rho-GTPase acting in polarized trafficking. Genetic analysis suggests that KIN1 and KIN2 act downstream of the Rab-GTPase Sec4, its exchange factor Sec2, and several components of the vesicle tethering complex, the Exocyst. We show that Kin1 and Kin2

APA, Harvard, Vancouver, ISO, and other styles

36

Masgrau, Aina, Andrea Battola, Trinidad Sanmartin, Leszek P. Pryszcz, Toni Gabaldón, and Manuel Mendoza. "Distinct roles of the polarity factors Boi1 and Boi2 in the control of exocytosis and abscission in budding yeast." Molecular Biology of the Cell 28, no. 22 (2017): 3082–94. http://dx.doi.org/10.1091/mbc.e17-06-0404.

Full text

Abstract:

Boi1 and Boi2 (Boi1/2) are budding yeast plasma membrane proteins that function in polarized growth, and in cytokinesis inhibition in response to chromosome bridges via the NoCut abscission checkpoint. How Boi1/2 act in these two distinct processes is not understood. We demonstrate that Boi1/2 are required for a late step in the fusion of secretory vesicles with the plasma membrane of the growing bud. Cells lacking Boi1/2 accumulate secretory vesicles and are defective in bud growth. In contrast, Boi2 is specifically required for abscission inhibition in cells with chromatin bridges. The SH3 d

APA, Harvard, Vancouver, ISO, and other styles

37

Nishida‐Fukuda, Hisayo. "The Exocyst: Dynamic Machine or Static Tethering Complex?" BioEssays 41, no. 8 (2019): 1900056. http://dx.doi.org/10.1002/bies.201900056.

Full text

APA, Harvard, Vancouver, ISO, and other styles

38

Donovan, Kirk W., and Anthony Bretscher. "Tracking individual secretory vesicles during exocytosis reveals an ordered and regulated process." Journal of Cell Biology 210, no. 2 (2015): 181–89. http://dx.doi.org/10.1083/jcb.201501118.

Full text

Abstract:

Post-Golgi secretory vesicle trafficking is a coordinated process, with transport and regulatory mechanisms to ensure appropriate exocytosis. While the contributions of many individual regulatory proteins to this process are well studied, the timing and dependencies of events have not been defined. Here we track individual secretory vesicles and associated proteins in vivo during tethering and fusion in budding yeast. Secretory vesicles tether to the plasma membrane very reproducibly for ∼18 s, which is extended in cells defective for membrane fusion and significantly lengthened and more varia

APA, Harvard, Vancouver, ISO, and other styles

39

Boehm, Cordula, and Mark C. Field. "Evolution of late steps in exocytosis: conservation and specialization of the exocyst complex." Wellcome Open Research 4 (November 29, 2019): 112. http://dx.doi.org/10.12688/wellcomeopenres.15142.2.

Full text

Abstract:

Background: The eukaryotic endomembrane system most likely arose via paralogous expansions of genes encoding proteins that specify organelle identity, coat complexes and govern fusion specificity. While the majority of these gene families were established by the time of the last eukaryotic common ancestor (LECA), subsequent evolutionary events has moulded these systems, likely reflecting adaptations retained for increased fitness. As well as sequence evolution, these adaptations include loss of otherwise canonical components, the emergence of lineage-specific proteins and paralog expansion. Th

APA, Harvard, Vancouver, ISO, and other styles

40

Boehm, Cordula, and Mark C. Field. "Evolution of late steps in exocytosis: conservation, specialization." Wellcome Open Research 4 (July 26, 2019): 112. http://dx.doi.org/10.12688/wellcomeopenres.15142.1.

Full text

Abstract:

Background: The eukaryotic endomembrane system likely arose via paralogous expansion of genes encoding proteins specifying organelle identity, coat complexes and government of fusion specificity. While the majority of these gene families were established by the time of the last eukaryotic common ancestor (LECA), subsequent evolutionary events molded these systems, likely reflecting adaptations retained for increased fitness. As well as sequence evolution, these adaptations include loss of otherwise canonical subunits, emergence of lineage-specific proteins and paralog expansion. The exocyst co

APA, Harvard, Vancouver, ISO, and other styles

41

He, Bing, Fengong Xi, Jian Zhang, Daniel TerBush, Xiaoyu Zhang, and Wei Guo. "Exo70p mediates the secretion of specific exocytic vesicles at early stages of the cell cycle for polarized cell growth." Journal of Cell Biology 176, no. 6 (2007): 771–77. http://dx.doi.org/10.1083/jcb.200606134.

Full text

Abstract:

In budding yeast, two classes of post-Golgi secretory vesicles carrying different sets of cargoes typified by Bgl2p and invertase are delivered to the plasma membrane for secretion. The exocyst is implicated in tethering these vesicles to the daughter cell membrane for exocytosis. In this study, we report that mutations in the exocyst component Exo70p predominantly block secretion of the Bgl2p vesicles. Furthermore, a defect in invertase vesicle trafficking caused by vps1Δ or pep12Δ in the exo70 mutant background is detrimental to the cell. The secretion defect in exo70 mutants was most pronou

APA, Harvard, Vancouver, ISO, and other styles

42

Munson, Mary, Dante Lepore, Michael Feyder, et al. "Exocyst Tethering Complex Regulation of SNARE Proteins and Membrane Fusion." Biophysical Journal 118, no. 3 (2020): 340a—341a. http://dx.doi.org/10.1016/j.bpj.2019.11.1896.

Full text

APA, Harvard, Vancouver, ISO, and other styles

43

Munson, Mary, Dante Lepore, Michael Feyder, et al. "Activation of the Exocyst Tethering Complex for SNARE Complex Regulation and Membrane Fusion." FASEB Journal 34, S1 (2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.00212.

Full text

APA, Harvard, Vancouver, ISO, and other styles

44

Lees, Joshua A., Calvin K. Yip, Thomas Walz, and Frederick M. Hughson. "Molecular organization of the COG vesicle tethering complex." Nature Structural & Molecular Biology 17, no. 11 (2010): 1292–97. http://dx.doi.org/10.1038/nsmb.1917.

Full text

APA, Harvard, Vancouver, ISO, and other styles

45

Mukherjee, Debarati, Arpita Sen, and R. Claudio Aguilar. "RhoGTPase-binding proteins, the exocyst complex and polarized vesicle trafficking." Small GTPases 5, no. 4 (2014): e983870. http://dx.doi.org/10.4161/sgtp.28453.

Full text

APA, Harvard, Vancouver, ISO, and other styles

46

Zhang, Xiaoyu, Erfei Bi, Peter Novick, et al. "Cdc42 Interacts with the Exocyst and Regulates Polarized Secretion." Journal of Biological Chemistry 276, no. 50 (2001): 46745–50. http://dx.doi.org/10.1074/jbc.m107464200.

Full text

Abstract:

Polarized delivery and incorporation of proteins and lipids to specific domains of the plasma membrane is fundamental to a wide range of biological processes such as neuronal synaptogenesis and epithelial cell polarization. The exocyst complex is specifically localized to sites of active exocytosis and plays essential roles in secretory vesicle targeting and docking at the plasma membrane. Sec3p, a component of the exocyst, is thought to be a spatial landmark for polarized exocytosis. In a search for proteins that regulate the localization of the exocyst in the budding yeastSaccharomyces cerev

APA, Harvard, Vancouver, ISO, and other styles

47

Jose, Mini, Sylvain Tollis, Deepak Nair, et al. "A quantitative imaging-based screen reveals the exocyst as a network hub connecting endocytosis and exocytosis." Molecular Biology of the Cell 26, no. 13 (2015): 2519–34. http://dx.doi.org/10.1091/mbc.e14-11-1527.

Full text

Abstract:

The coupling of endocytosis and exocytosis underlies fundamental biological processes ranging from fertilization to neuronal activity and cellular polarity. However, the mechanisms governing the spatial organization of endocytosis and exocytosis require clarification. Using a quantitative imaging-based screen in budding yeast, we identified 89 mutants displaying defects in the localization of either one or both pathways. High-resolution single-vesicle tracking revealed that the endocytic and exocytic mutants she4∆ and bud6∆ alter post-Golgi vesicle dynamics in opposite ways. The endocytic and

APA, Harvard, Vancouver, ISO, and other styles

48

Essid, Miriam, Navin Gopaldass, Kunito Yoshida, Christien Merrifield, and Thierry Soldati. "Rab8a regulates the exocyst-mediated kiss-and-run discharge of the Dictyostelium contractile vacuole." Molecular Biology of the Cell 23, no. 7 (2012): 1267–82. http://dx.doi.org/10.1091/mbc.e11-06-0576.

Full text

Abstract:

Water expulsion by the contractile vacuole (CV) in Dictyostelium is carried out by a giant kiss-and-run focal exocytic event during which the two membranes are only transiently connected but do not completely merge. We present a molecular dissection of the GTPase Rab8a and the exocyst complex in tethering of the contractile vacuole to the plasma membrane, fusion, and final detachment. Right before discharge, the contractile vacuole bladder sequentially recruits Drainin, a Rab11a effector, Rab8a, the exocyst complex, and LvsA, a protein of the Chédiak–Higashi family. Rab8a recruitment precedes

APA, Harvard, Vancouver, ISO, and other styles

49

Yu, Sidney, Ayano Satoh, Marc Pypaert, Karl Mullen, Jesse C. Hay, and Susan Ferro-Novick. "mBet3p is required for homotypic COPII vesicle tethering in mammalian cells." Journal of Cell Biology 174, no. 3 (2006): 359–68. http://dx.doi.org/10.1083/jcb.200603044.

Full text

Abstract:

TRAPPI is a large complex that mediates the tethering of COPII vesicles to the Golgi (heterotypic tethering) in the yeast Saccharomyces cerevisiae. In mammalian cells, COPII vesicles derived from the transitional endoplasmic reticulum (tER) do not tether directly to the Golgi, instead, they appear to tether to each other (homotypic tethering) to form vesicular tubular clusters (VTCs). We show that mammalian Bet3p (mBet3p), which is the most highly conserved TRAPP subunit, resides on the tER and adjacent VTCs. The inactivation of mBet3p results in the accumulation of cargo in membranes that col

APA, Harvard, Vancouver, ISO, and other styles

50

Mukherjee, Indrani, and Charles Barlowe. "Overexpression of Sly41 suppresses COPII vesicle–tethering deficiencies by elevating intracellular calcium levels." Molecular Biology of the Cell 27, no. 10 (2016): 1635–49. http://dx.doi.org/10.1091/mbc.e15-10-0704.

Full text

Abstract:

SLY41 was identified as a multicopy suppressor of loss of Ypt1, a Rab GTPase essential for COPII vesicle tethering at the Golgi complex. SLY41 encodes a polytopic membrane protein with homology to a class of solute transporter proteins, but how overexpression suppresses vesicle-tethering deficiencies is not known. Here we show that Sly41 is efficiently packaged into COPII vesicles and actively cycles between the ER and Golgi compartments. SLY41 displays synthetic negative genetic interactions with PMR1, which encodes the major Golgi-localized Ca2+/Mn2+transporter and suggests that Sly41 influe

APA, Harvard, Vancouver, ISO, and other styles

We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!