EHD1 Interacts with Retromer to Stabilize SNX1 Tubules and Facilitate Endosome‐to‐Golgi Retrieval

Gokool, Suzanne; Tattersall, Daniel; Seaman, Matthew N.

doi:10.1111/j.1600-0854.2007.00652.x

Cited by 122 publications

(145 citation statements)

References 52 publications

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“…8A, we confirmed this observation and found that these tubules were also positive for VPS26, which we rarely observe tubule-associated. Previously, we have reported that the EHD1 protein is required to stabilise SNX1 tubules and thereby facilitates endosome-to-Golgi retrieval (Gokool et al, 2007a). Therefore, we carried out a morphometric analysis of the SNX1 and VPS26 tubules in cells that had undergone KDs of strumpellin, KIAA1033, WASH1, EHD1 or a double KD of KIAA1033 and EHD1.…”

Section: The Wash1 Complex Regulates Endosomal Tubulesmentioning

confidence: 99%

“…Initially, using a cell line expressing a CD8-CIMPR reporter and our antibodyuptake assay (Seaman, 2004;Seaman, 2007;Gokool et al, 2007a;Seaman et al, 2009), we examined endosome-to-Golgi retrieval after cells had been treated with siRNA to KD both VPS26 and VPS35 or strumpellin and KIAA1033. The VPS26 and VPS35 double KD resulted in the endocytosed antibody accumulating in peripheral structures but the strumpellin and KIAA1033 double KD did not appear to strongly inhibit endosome-to-Golgi retrieval as the endocytosed anti-CD8 colocalised with TGN46 (Fig.…”

Section: The Role Of the Retromer-interacting Proteins In Endosometo-mentioning

confidence: 99%

“…In yeast, the SNX3 homologue Grd19p binds to Ftr1p to sort Ftr1p into the retromer pathway (Strochlic et al, 2008). In mammalian cells, the EPS15 homology domain protein, EHD1, interacts with retromer and is required to stabilize SNX1-positive membrane tubules (Gokool et al, 2007a). Recruitment of the cargo-selective retromer complex to the endosomal membrane is mediated by the small GTPase RAB7 (Rojas et al, 2008;Seaman et al, 2009).…”

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The cargo-selective retromer complex is a recruiting hub for protein complexes that regulate endosomal tubule dynamics

Harbour

Breusegem

Antrobus³

et al. 2010

Journal of Cell Science

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Research Article 3703 IntroductionEndosomal protein sorting has a vital role in a number of physiologically important processes including antigen presentation, macromolecular nutrient uptake, growth factor receptor signaling and downregulation, autophagy and lysosome biogenesis (for reviews, see Sadowski et al., 2009;Saksena and Emr, 2009;Sann et al., 2009;Seaman, 2008;Lee et al., 2008). Recent studies of inherited diseases have identified several examples of genes encoding proteins that function in endosomal protein sorting that, when mutated, result in a range of pathologies. A notable example is hereditary spastic paraplegias (HSP), the hallmark of which is a selective distal axonopathy. There is a striking localisation of many of the HSP-encoded proteins to the endosome, including the microtubule-severing protein spastin, the ubiquitin-ligase-interacting protein spartin, and NIPA1, a membrane protein that mediates bone morphogenic protein signaling at the endosome (Tsang et al., 2009; for a review, see Salinas et al., 2008). Despite this concentration of HSP proteins at endosomes, in most cases their function is unknown.Much of the core machinery that carries out endosomal protein sorting is conserved in evolution, for example, the retromer complex (for reviews, see Attar and Cullen, 2009;Verges, 2008;Collins, 2008;Bonifacino and Hurley, 2008). Retromer mediates endosometo-Golgi retrieval of lysosomal and vacuolar hydrolase receptors (e.g. the cation-independent mannose 6 phosphate receptor, CIMPR) along with other physiologically significant membrane proteins including wntless, which functions in WNT secretion, and SORL1, a protein that is genetically linked to late-onset Alzheimer's disease (Arighi et al., 2004;Seaman, 2004;Eaton, 2008;Nielsen et al., 2007;Rogaeva et al., 2007).The retromer complex was first identified in yeast where it comprises five proteins encoded by vacuolar protein sorting (VPS) genes. The heteropentameric retromer complex can be functionally dissected into two subcomplexes: a cargo-selective complex formed from a conserved trimer of Vps35p, Vps29p and Vps26p and a 'structural complex' formed from a dimer of the sorting nexin (SNX) proteins Vps5p and Vps17p (Seaman et al., 1998). In mammals, SNX1, SNX2 with SNX5 and SNX6 provide the 'structural' role and can tubulate membranes through the C-terminal Bin, amphiphysin and Rvs (BAR) domains present in these proteins (Carlton et al., 2004;Wassmer et al., 2007). Additionally, SNX5 and SNX6 interact with the microtubule cytoskeleton via the p150glued protein that binds to dynein, thereby linking endosomal protein sorting to microtubules (Wassmer et al., 2009;Hong et al., 2009).The interaction between the SNX component of retromer and p150glued is an example of how retromer-interacting proteins facilitate retromer in mediating endosome-to-Golgi retrieval. In yeast, the SNX3 homologue Grd19p binds to Ftr1p to sort Ftr1p into the retromer pathway (Strochlic et al., 2008). In mammalian cells, the EPS15 homology domain protein, EHD1, interacts ...

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Section: The Wash1 Complex Regulates Endosomal Tubulesmentioning

confidence: 99%

Section: The Role Of the Retromer-interacting Proteins In Endosometo-mentioning

confidence: 99%

mentioning

confidence: 99%

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The cargo-selective retromer complex is a recruiting hub for protein complexes that regulate endosomal tubule dynamics

Harbour

Breusegem

Antrobus³

et al. 2010

Journal of Cell Science

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“…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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“…The SNX dimer, currently understood to comprise a combination of SNX1 or SNX2 with SNX5 or SNX6 (Wassmer et al, 2007), binds to phosphoinositol 3-phosphate through its phox homology domains and induces membrane curvature by the action of its C-terminal BAR (BinAmphiphysin-Rvs) domains (Kurten et al, 2001;Cheever et al, 2001;Yu and Lemmon, 2001;Cozier et al, 2002;Carlton et al, 2004). The tubules generated by the SNX dimer are stabilised by EHD1 (also known as RME-1), which associates with the CSC (Gokool et al, 2007b;Zhang et al, 2012). Although SNX5 and SNX6 do not drive membrane tubulation (van Weering et al, 2012), both interact with the p150Glued component of dynactin (Wassmer et al, 2009;Hong et al, 2009) and, therefore, link retromer-mediated protein sorting with microtubules through dynein.…”

Section: Introductionmentioning

confidence: 99%

RME-8 coordinates the WASH complex with the retromer SNX-BAR dimer to control endosomal tubulation

Freeman

Hesketh

Seaman

2014

Journal of Cell Science

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102

100

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Retromer is a vital element of the endosomal protein sorting machinery and comprises two subcomplexes that operate together to sort membrane proteins (cargo) and tubulate membranes. Tubules are formed by a dimer of sorting nexins, a key component of which is SNX1. Cargo selection is mediated by the VPS35-VPS29-VPS26 trimer, which additionally recruits the WASH complex through VPS35 binding to the WASH complex subunit FAM21. Loss of function of the WASH complex leads to dysregulation of endosome tubulation, although it is unclear how this occurs. Here, we show that FAM21 also binds to the SNX1-interacting DNAJ protein RME-8. Loss of RME-8 causes altered kinetics of SNX1 membrane association and a pronounced increase in highly branched endosomal tubules. Building on previous observations from other laboratories, we show that these tubules contain membrane proteins that are dependent upon WASH complex activity for their localization to the plasma membrane. Therefore, we propose that the interaction between RME-8 and the WASH complex provides a means to coordinate the activity of the WASH complex with the membrane-tubulating function of the sorting nexins at sites where retromer-mediated endosomal protein sorting occurs.

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EHD1 Interacts with Retromer to Stabilize SNX1 Tubules and Facilitate Endosome‐to‐Golgi Retrieval

Cited by 122 publications

References 52 publications

The cargo-selective retromer complex is a recruiting hub for protein complexes that regulate endosomal tubule dynamics

The cargo-selective retromer complex is a recruiting hub for protein complexes that regulate endosomal tubule dynamics

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

RME-8 coordinates the WASH complex with the retromer SNX-BAR dimer to control endosomal tubulation

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