rab4 Regulates Transport to the Apical Plasma Membrane in Madin-Darby Canine Kidney Cells

Mohrmann, Karin; Leijendekker, R.; Gerez, Lisya; Sluijs, Peter van der

doi:10.1074/jbc.m111237200

Cited by 40 publications

(42 citation statements)

References 51 publications

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Section: Introductionsupporting

confidence: 82%

“…Indeed, AP-1B was found to mediate specific basolateral recycling from endosomes (Gan et al, 2002), supporting earlier proposals that implicated clathrin/AP-1 coats in polarized cells in recycling transferrin receptor back to the basolateral surface (Futter et al, 1998). Consistent with this, BFA treatment caused loss of polarity in recycling to the cell surface in Madin-Darby canine kidney (MDCK) cells (Futter et al, 1998;Mohrmann et al, 2002).The apparent discrepancy between experimental results and their interpretations may be due to the complexity and plasticity of the endosomal system. Long-term experiments such as overexpression or elimination of proteins, which takes hours to days to take effect, may cause indirect effects or adaptation.…”

supporting

confidence: 83%

“…Three rab proteins have been implicated in regulating receptor recycling. Rab4 was implicated in regulating recycling from endosomes to the cell surface in nonpolarized and to the apical surface in polarized cells (van der Sluijs et al, 1992;Mohrmann et al, 2002;Deneka et al, 2003).…”

Section: Ap-1a/clathrin Coats Mediate Receptor Recyclingmentioning

confidence: 99%

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In Vitro Formation of Recycling Vesicles from Endosomes Requires Adaptor Protein-1/Clathrin and Is Regulated by Rab4 and the Connector Rabaptin-5

Pagano

Crottet

Prescianotto-Baschong

et al. 2004

MBoC

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The involvement of clathrin and associated adaptor proteins in receptor recycling from endosomes back to the plasma membrane is controversial. We have used an in vitro assay to identify the molecular requirements for the formation of recycling vesicles. Cells expressing the asialoglycoprotein receptor H1, a typical recycling receptor, were surface biotinylated and then allowed to endocytose for 10 min. After stripping away surface-biotin, the cells were permeabilized and the cytosol washed away. In a temperature-, cytosol-, and nucleotide-dependent manner, the formation of sealed vesicles containing biotinylated H1 could be reconstituted. Vesicle formation was strongly inhibited upon immunodepletion of adaptor protein (AP)-1, but not of AP-2 or AP-3, from the cytosol, and was restored by readdition of purified AP-1. Vesicle formation was stimulated by supplemented clathrin, but inhibited by brefeldin A, consistent with the involvement of ARF1 and a brefeldin-sensitive guanine nucleotide exchange factor. The GTPase rab4, but not rab5, was required to generate endosome-derived vesicles. Depletion of rabaptin-5/rabex-5, a known interactor of both rab4 and ␥-adaptin, stimulated and addition of the purified protein strongly inhibited vesicle production. The results indicate that recycling is mediated by AP-1/clathrin-coated vesicles and regulated by rab4 and rabaptin-5/rabex-5. INTRODUCTIONEarly endosomes are a major sorting station for proteins and membranes in eukaryotic cells (Gruenberg, 2001;Maxfield and McGraw, 2004). They receive material from the cell surface by endocytosis and from the exocytic pathway via the trans-Golgi network (TGN), and they distribute it further to late endosomes and back to the TGN and the plasma membrane. Transport receptors like the transferrin receptor, the low-density lipoprotein (LDL) receptor, and the asialoglycoprotein (ASGP) receptor cycle continuously between the plasma membrane and early endosomes (Spiess, 1990;Trowbridge et al., 1993). Receptor-positive early endosomes can be subdivided into sorting endosomes and recycling endosomes (or endocytic recycling compartment, ERC). Primary endocytic vesicles fuse to sorting endosomes where ligands dissociate from their receptors because of a reduced internal pH. The receptors exit into tubular membranes that form recycling endosomes, whereas the ligands with the main fluid volume mature to late endosomes ("geometrybased sorting"; Maxfield and McGraw, 2004). There seem to be two main recycling pathways from early endosomes to the plasma membrane: a fast one directly from sorting endosomes and a slower one via recycling endosomes (Sheff et al., 1999;Hao and Maxfield, 2000;.The mechanisms to generate endosome-derived recycling vesicles are not clear, because there are seemingly contradictory findings. In general, formation of transport vesicles between organelles of the endocytic and secretory pathways requires cytosolic coat proteins to be recruited at the membrane of the donor compartment. Among the established coat complexes, clathr...

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Section: Introductionsupporting

confidence: 82%

supporting

confidence: 83%

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In Vitro Formation of Recycling Vesicles from Endosomes Requires Adaptor Protein-1/Clathrin and Is Regulated by Rab4 and the Connector Rabaptin-5

Pagano

Crottet

Prescianotto-Baschong

et al. 2004

MBoC

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“…In nonpolarized cells Rab4 is primarily associated with early endosomes and is thought to contribute to direct transport from early endosomes to the plasma membrane as well as early endosome to recycling endosome transport (Sheff et al, 1999). In MDCK cells Rab4 has also been reported to associate with early endosomes and a later compartment named the common endosome, where is promotes apical delivery of transcytotic cargo (Mohrmann et al, 2002). Rab11 is primarily associated with recycling endosomes and has been reported to act after Rab4 in nonpolarized cells, mediating recycling endosome to PM transport of clathrin-dependent and clathrin-independent recycling cargo (Sheff et al, 1999;Weigert et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

RAB-10 Is Required for Endocytic Recycling in theCaenorhabditis elegansIntestine

Chen

Schweinsberg

Vashist

et al. 2006

MBoC

190

385

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The endocytic pathway of eukaryotes is essential for the internalization and trafficking of macromolecules, fluid, membranes, and membrane proteins. One of the most enigmatic aspects of this process is endocytic recycling, the return of macromolecules (often receptors) and fluid from endosomes to the plasma membrane. We have previously shown that the EH-domain protein RME-1 is a critical regulator of endocytic recycling in worms and mammals. Here we identify the RAB-10 protein as a key regulator of endocytic recycling upstream of RME-1 in polarized epithelial cells of the Caenorhabditis elegans intestine. rab-10 null mutant intestinal cells accumulate abnormally abundant RAB-5-positive early endosomes, some of which are enlarged by more than 10-fold. Conversely most RME-1-positive recycling endosomes are lost in rab-10 mutants. The abnormal early endosomes in rab-10 mutants accumulate basolaterally recycling transmembrane cargo molecules and basolaterally recycling fluid, consistent with a block in basolateral transport. These results indicate a role for RAB-10 in basolateral recycling upstream of RME-1. We found that a functional GFP-RAB-10 reporter protein is localized to endosomes and Golgi in wild-type intestinal cells consistent with a direct role for RAB-10 in this transport pathway. INTRODUCTIONEndocytosis and endocytic trafficking controls the uptake and sorting of extracellular macromolecules as well as the components of the cell membrane itself, counterbalancing secretion and allowing a complex interplay between cells and their environment that is important for a myriad of cellular activities (Brodsky et al., 2001;Maxfield and McGraw, 2004). The steps involved in the uptake and trafficking of cargo within the endosomal system have been well described, but many of the components mediating these steps at the molecular level remain to be identified (Brodsky et al., 2001;Maxfield and McGraw, 2004). Many receptors and their associated ligands cluster into clathrincoated pits, whereas other types of cargo utilize clathrinindependent uptake mechanisms (Nichols, 2003;Gesbert et al., 2004). Plasma membrane invaginations pinch off into vesicles, uncoat, and then fuse with one another and with early endosomes. In early endosomes some ligand-receptor complexes dissociate because of the reduced pH of the endosomal lumen (Mukherjee et al., 1997). Many receptors then recycle to the plasma membrane (PM) either directly or indirectly via recycling endosomes (Mukherjee et al., 1997;Maxfield and McGraw, 2004). Many ligands do not recycle but instead are transported from early to late endosomes and eventually to lysosomes for degradation (Mukherjee et al., 1997). In polarized epithelial cells such as cultured Madin-Darby canine kidney (MDCK) cells, an additional layer of complexity in the endocytic pathway contributes to formation and/or maintenance of the specialized apical and basolateral domains (Nelson and Yeaman, 2001;Mostov et al., 2003;Hoekstra et al., 2004). Both the apical and basolateral membranes deliver cargo ...

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“…Protein sorting in recycling endosomes depends upon the function of the small GTPase Rab4, a close homologue of Rab11 (Li, et al, 2008;Ward, et al, 2005). Rab3 also has a role in anterograde traffic between the trans-Golgi network and recycling endosomes (Mohrmann, et al, 2002;van der Sluijs, et al, 1992). The Rab small GTPases, Sec4 in yeast and Rab11 in metazoans, facilitate trafficking of secretory vesicles carrying Sec15-exocyst components from recycling endosomes to the plasma membrane (Langevin, et al, 2005).…”

Section: Rab Gtpases and Vesicular Tetheringmentioning

confidence: 99%

Molecular Machinery Regulating Exocytosis

Shandala¹,

Kakavanos-Plew²,

Ng³

et al. 2012

Crosstalk and Integration of Membrane Trafficking Pathways

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rab4 Regulates Transport to the Apical Plasma Membrane in Madin-Darby Canine Kidney Cells

Cited by 40 publications

References 51 publications

In Vitro Formation of Recycling Vesicles from Endosomes Requires Adaptor Protein-1/Clathrin and Is Regulated by Rab4 and the Connector Rabaptin-5

In Vitro Formation of Recycling Vesicles from Endosomes Requires Adaptor Protein-1/Clathrin and Is Regulated by Rab4 and the Connector Rabaptin-5

RAB-10 Is Required for Endocytic Recycling in theCaenorhabditis elegansIntestine

Molecular Machinery Regulating Exocytosis

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