Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo

Wu, Shu-Ya; Mehta, Sunil; Pichaud, Franck; Bellen, Hugo J.; Quiocho, Florante A.

doi:10.1038/nsmb987

Cited by 248 publications

(246 citation statements)

References 45 publications

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“…A previous study on MDCK cells suggested that the exocyst, through its Sec15 component, may function as a Rab11 effector to regulate basolateral-to-apical transcytosis (23). The sec15 mutant in the fly photoreceptor results in strong accumulation of Rab11 within the apical membranes of the photoreceptor (22). We confirmed the accumulation of RAB-11-positive vesicles at the apical PM in sec-10 mutants (Fig.…”

Section: Dual Involvement Of Sec-10 In Apical and Basolateral Endosomalsupporting

confidence: 76%

“…Consistent with this idea, the exocyst localizes to the PM where exocytosis actively occurs and has been implicated in many cellular trafficking processes including polarized budding in yeast (14), neurite growth in neurons (15), GLUT4 membrane insertion in fat cells (16), and cell migration (17)(18)(19). Recent studies have revealed an association between the exocyst and recycling endosome-localized proteins, such as Arf6 (20), AP1B (21), and Rab11 (22), and the presence of exocyst on multiple populations of endosomes (23). Interfering with exocyst functions affects several endocytic pathways, such as transferrin receptor (TfR) recycling in nonpolarized cells (20), and apical and basolateral recycling in polarized cells (23,24).…”

mentioning

confidence: 60%

“…We verified by immunofluorescence microscopy that endogenous SEC-15, a vesicle-associated component of the exocyst (22,46), partially colocalized with hTAC tubules at the branching point or at/near the end of a tubule (Fig. S8A).…”

Section: Sec-10 Is Specifically Involved In Intermediatementioning

confidence: 89%

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SEC-10 and RAB-10 coordinate basolateral recycling of clathrin-independent cargo through endosomal tubules in Caenorhabditis elegans

Chen

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Despite the increasing number of regulatory proteins identified in clathrin-independent endocytic (CIE) pathways, our understanding of the exact functions of these proteins and the sequential manner in which they function remains limited. In this study, using the Caenorhabditis elegans intestine as a model, we observed a unique structure of interconnected endosomal tubules, which is required for the basolateral recycling of several CIE cargoes including hTAC, GLUT1, and DAF-4. SEC-10 is a subunit of the octameric protein complex exocyst. Depleting SEC-10 and several other exocyst components disrupted the endosomal tubules into various ring-like structures. An epistasis analysis further suggested that SEC-10 operates at the intermediate step between early endosomes and recycling endosomes. The endosomal tubules were also sensitive to inactivation of the Rab GTPase RAB-10 and disruption of microtubules. Taken together, our data suggest that SEC-10 coordinates with RAB-10 and microtubules to form the endosomal tubular network for efficient recycling of particular CIE cargoes.endosomal tubules | recycling | microtubule | clathrin-independent endocytosis | live worm imaging

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Section: Dual Involvement Of Sec-10 In Apical and Basolateral Endosomalsupporting

confidence: 76%

mentioning

confidence: 60%

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SEC-10 and RAB-10 coordinate basolateral recycling of clathrin-independent cargo through endosomal tubules in Caenorhabditis elegans

Chen

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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“…Through this interaction, Sec4 controls the assembly of the exocyst complex that is needed for the tethering of secretory vesicles at the plasma membrane. In other eukaryotes, Rab proteins such as Rab11 and Rab8, which are implicated in membrane trafficking to the plasma membrane, were also shown to interact with Sec15 (Zhang et al 2004;Wu et al 2005;Oztan et al 2007). Together, these studies suggest that the exocyst functions as a downstream effector of Rab proteins to mediate vesicle tethering at the plasma membrane in eukaryotic cells.…”

Section: The Rab Family Of Small Gtp-binding Proteinsmentioning

confidence: 69%

Membrane Organization and Dynamics in Cell Polarity

Orlando¹,

Guo²

2009

Cold Spring Harbor Perspectives in Biology

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The establishment and maintenance of cell polarity is important to a wide range of biological processes ranging from chemotaxis to embryogenesis. An essential feature of cell polarity is the asymmetric organization of proteins and lipids in the plasma membrane. In this article, we discuss how polarity regulators such as small GTP-binding proteins and phospholipids spatially and kinetically control vesicular trafficking and membrane organization. Conversely, we discuss how membrane trafficking contributes to cell polarization through delivery of polarity determinants and regulators to the plasma membrane.

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“…We found that the Sec15 subunit is polarized during cell migration. Because Sec15 is a Rab11 binding protein (15,16), we tested further the relationship between these two proteins. We found that Sec15 polarity is controlled by rab11 activity and that sec15 and other subunits of the exocyst are necessary for the spatial restriction of RTK activity and for border cell migration.…”

mentioning

confidence: 99%

Spatial restriction of receptor tyrosine kinase activity through a polarized endocytic cycle controls border cell migration

Assaker

Ramel²,

Wculek³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

107

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Border cell migration is a stereotyped migration occurring during the development of the Drosophila egg chamber. During this process, a cluster composed of six to eight follicle cells migrates between nurse cells toward the oocyte. Receptor tyrosine kinases (RTKs) are enriched at the leading edge of the follicle cells and establish the directionality of their migration. Endocytosis has been shown to play a role in the maintenance of this polarization; however, the mechanisms involved are largely unknown. In this study, we show that border cell migration requires the function of the small GTPases Rab5 and Rab11 that regulate trafficking through the early and the recycling endosome, respectively. Expression of a dominant negative form of rab11 induces a loss of the polarization of RTK activity, which correlates with a severe migration phenotype. In addition, we demonstrate that the exocyst component Sec15 is distributed in structures that are polarized during the migration process in a Rab11-dependent manner and that the down-regulation of different subunits of the exocyst also affects migration. Together, our data demonstrate a fundamental role for a plasma membrane-endosome trafficking cycle in the maintenance of active RTK at the leading edge of border cells during their migration.

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Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo

Cited by 248 publications

References 45 publications

SEC-10 and RAB-10 coordinate basolateral recycling of clathrin-independent cargo through endosomal tubules in Caenorhabditis elegans

SEC-10 and RAB-10 coordinate basolateral recycling of clathrin-independent cargo through endosomal tubules in Caenorhabditis elegans

Membrane Organization and Dynamics in Cell Polarity

Spatial restriction of receptor tyrosine kinase activity through a polarized endocytic cycle controls border cell migration

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