Rme-1 regulates the distribution and function of the endocytic recycling compartment in mammalian cells

Lin, Sharron X.; Grant, Barth D.; Hirsh, David; Maxfield, Frederick R.

doi:10.1038/35078543

Cited by 238 publications

(302 citation statements)

References 38 publications

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“…These expression data suggest a functional significance of EHD2 expression in the context of GLUT4 trafficking. Consistent with this possibility, recent studies with EHD1 and its Caenorhabditis elegans homolog RME-1 suggest that these proteins are part of the molecular machinery responsible for recycling of receptors to the plasma membrane (32)(33)(34). Furthermore, connections between EHD1 and endocytosis of IGF-1 receptor in Chinese hamster ovary cells has been described (35).…”

Section: Identification Of Ehd2 In Membrane Fractions From 3t3-l1supporting

confidence: 51%

EHD2 and the Novel EH Domain Binding Protein EHBP1 Couple Endocytosis to the Actin Cytoskeleton

Guilherme

Soriano

Bose

et al. 2004

Journal of Biological Chemistry

139

181

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Here we identified two novel proteins denoted EH domain protein 2 (EHD2) and EHD2-binding protein 1 (EHBP1) that link clathrin-mediated endocytosis to the actin cytoskeleton. EHD2 contains an N-terminal P-loop and a C-terminal EH domain that interacts with NPF repeats in EHBP1. Disruption of EHD2 or EHBP1 function by small interfering RNA-mediated gene silencing inhibits endocytosis of transferrin into EEA1-positive endosomes as well as GLUT4 endocytosis into cultured adipocytes. EHD2 localizes with cortical actin filaments, whereas EHBP1 contains a putative actin-binding calponin homology domain. High expression of EHD2 or EHBP1 in intact cells mediates extensive actin reorganization. Thus EHD2 appears to connect endocytosis to the actin cytoskeleton through interactions of its N-terminal domain with membranes and its C-terminal EH domain with the novel EHBP1 protein.

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Section: Identification Of Ehd2 In Membrane Fractions From 3t3-l1supporting

confidence: 51%

EHD2 and the Novel EH Domain Binding Protein EHBP1 Couple Endocytosis to the Actin Cytoskeleton

Guilherme

Soriano

Bose

et al. 2004

Journal of Biological Chemistry

139

181

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“…Thus our studies of worm RAB-10 are very likely to be highly applicable to understanding Rab10 function in mammalian systems. The intestinal phenotype caused by loss of rab-10 is very similar to that caused by loss of rme-1, a known endocytic recycling factor Lin et al, 2001). However, unlike rme-1 mutants that also display obvious endocytic defects in oocytes and coelomocytes, we did not detect endocytic defects in oocytes or coelomocytes in rab-10 mutant worms.…”

Section: Rab-10 Is Required For Endocytic Recycling In the Worm Intesmentioning

confidence: 36%

“…Equivalent GFP-fusions for these three proteins have previously been shown to be functional and traffic normally in mammalian cells and/or C. elegans. First we expressed the human transferrin receptor (hTfR-GFP), a marker for clathrin-dependent uptake and rme-1-dependent recycling in mammalian cells (Yamashiro et al, 1984;Burack et al, 2000;Lin et al, 2001). Next we expressed the ␣-chain of the human IL-2 receptor TAC (hTAC-GFP), a marker for clathrin-independent endocytosis and rme-1-dependent recycling in mammalian cells (Caplan et al, 2002;Naslavsky et al, 2004).…”

Section: Gum-1 Mutants Display Rme-1-like Endocytosis Defects In the mentioning

confidence: 99%

RAB-10 Is Required for Endocytic Recycling in theCaenorhabditis elegansIntestine

Chen

Schweinsberg

Vashist

et al. 2006

MBoC

187

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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“…Golgi transport (20,21). Importantly, we found that loss of RME-1 resulted in dramatically different defects in the subcellular localization of SMA-6 and DAF-4; DAF-4::GFP accumulated in intracellular vesicles, whereas overall levels of SMA-6:: GFP were severely reduced, suggesting that SMA-6 was being inappropriately degraded ( Fig.…”

Section: Clathrin-dependent Endocytosis Is Necessary For Bmp Receptormentioning

confidence: 76%

“…2 A, B, L, and M). Previous work indicated that a block in recycling to the plasma membrane via the ERC often results in intracellular trapping of receptors, whereas blocks in retromer-dependent recycling often results in missorting of receptors to the lysosome, where they are degraded (20,(22)(23)(24). Consistent with this idea, the accumulation of intracellular DAF-4 in the intestine of rme-1 mutants strongly resembled the accumulation of well-characterized ERC cargo hTAC::GFP (human IL-2 receptor α-chain) in rme-1 mutants (Fig.…”

Section: Clathrin-dependent Endocytosis Is Necessary For Bmp Receptormentioning

confidence: 99%

BMP signaling requires retromer-dependent recycling of the type I receptor

Gleason

Akintobi²,

Grant³

et al. 2014

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

105

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The transforming growth factor β (TGFβ) superfamily of signaling pathways, including the bone morphogenetic protein (BMP) subfamily of ligands and receptors, controls a myriad of developmental processes across metazoan biology. Transport of the receptors from the plasma membrane to endosomes has been proposed to promote TGFβ signal transduction and shape BMP-signaling gradients throughout development. However, how postendocytic trafficking of BMP receptors contributes to the regulation of signal transduction has remained enigmatic. Here we report that the intracellular domain of Caenorhabditis elegans BMP type I receptor SMA-6 (small-6) binds to the retromer complex, and in retromer mutants, SMA-6 is degraded because of its missorting to lysosomes. Surprisingly, we find that the type II BMP receptor, DAF-4 (dauer formation-defective-4), is retromer-independent and recycles via a distinct pathway mediated by ARF-6 (ADP-ribosylation factor-6). Importantly, we find that loss of retromer blocks BMP signaling in multiple tissues. Taken together, our results indicate a mechanism that separates the type I and type II receptors during receptor recycling, potentially terminating signaling while preserving both receptors for further rounds of activation.endocytosis | receptor trafficking | C. elegans

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Rme-1 regulates the distribution and function of the endocytic recycling compartment in mammalian cells

Cited by 238 publications

References 38 publications

EHD2 and the Novel EH Domain Binding Protein EHBP1 Couple Endocytosis to the Actin Cytoskeleton

EHD2 and the Novel EH Domain Binding Protein EHBP1 Couple Endocytosis to the Actin Cytoskeleton

RAB-10 Is Required for Endocytic Recycling in theCaenorhabditis elegansIntestine

BMP signaling requires retromer-dependent recycling of the type I receptor

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