Evolutionary variations of VPS29, and their implications for the heteropentameric model of retromer

Harbour, Michael E.; Seaman, Matthew N.

doi:10.4161/cib.16855

Cited by 19 publications

(16 citation statements)

References 11 publications

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“…S2). It was shown that Vps29p S. cerevisiae also contains an additional ~80 amino acid loop, when compare with mammals, responsible for the greater affinity observed with Vps5p [50]. It is possible that, similar to Vps29 from other species, the extra C-terminal of GlVPS29 might be a scaffold for retromer interaction with accessory proteins [51].…”

Section: 0 Discussionmentioning

confidence: 99%

“…Finally, oligomerization of the subcomplexes into budding domains could serve to promote clustering of the complex and the receptor retrieval process. Further evidence of the function on the non-BAR GlSNXs, incapable of performing tubulation by themselves, are required to disclose whether they may function together with the cargo-selective subcomplex as an heteropentamer or rather as two independent subcomplexes for PV-to-ER receptor retrieval as suggested by Harbour et al [50, 51]. …”

Section: 0 Discussionmentioning

confidence: 99%

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The giardial VPS35 retromer subunit is necessary for multimeric complex assembly and interaction with the vacuolar protein sorting receptor

Miras

Merino

Gottig

et al. 2013

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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The retromer is a pentameric protein complex that mediates the retrograde transport of acid hydrolase receptors between endosomes and the trans-Golgi network and is conserved across all eukaryotes. Unlike other eukaryotes, the endomembrane system of Giardia trophozoite is simple and is composed only of the endoplasmic reticulum and peripheral vesicles (PVs), which may represent an ancient organellar system converging compartments such as early and late endosomes and lysosomes. Sorting and trafficking of membrane proteins and soluble hydrolases from the endoplasmic reticulum to the PVs has been described as specific and conserved but whether the giardial retromer participates in receptor recycling remains elusive. Homologs of the retromer Vacuolar Protein Sorting (Vps35p, Vps26p, and Vps29p) have been identified in this parasite. Cloning the GlVPS35 subunit and antisera production enabled the localization of this protein in the PVs as well as in the cytosol. Tagged expression of the subunits was used to demonstrate their association with membranes, and immunofluorescence confocal laser scanning revealed high degrees of colabeling between the retromer subunits and also with the endoplasmic reticulum and PV compartment markers. Protein-protein interaction data revealed interaction between the subunits and of GlVPS35 with the cytosolic domain of the hydrolase receptor GlVps. Altogether our data provide original information on the molecular interactions that mediate assembly of the cargo-selective retromer subcomplex and its involvement in the recycling of the acid hydrolase receptor in this parasite.

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Section: 0 Discussionmentioning

confidence: 99%

Section: 0 Discussionmentioning

confidence: 99%

The giardial VPS35 retromer subunit is necessary for multimeric complex assembly and interaction with the vacuolar protein sorting receptor

Miras

Merino

Gottig

et al. 2013

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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“…How and why yeast employ only minimal machinery for mediating endosome-to-Golgi retrieval is subject to speculation but a plausible explanation centres on evolutionary variation of the VPS29 gene that results in the gain of additional protein sequences very close to the region of Vps29 that mediates binding to TBC1D5 (Harbour and Seaman, 2011). It is also tempting to speculate that, in yeast, retromer function is restricted to the endosome-to-Golgi pathway and that, as a result, retromer-interacting proteins such as the WASH complex that are required for endosome-to-plasma membrane recycling have been lost.…”

Section: Evolutionary Conservation Of Retromerinteracting Proteinsmentioning

confidence: 99%

The retromer complex – endosomal protein recycling and beyond

Seaman

2012

Journal of Cell Science

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416

434

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SummaryThe retromer complex is a vital element of the endosomal protein sorting machinery that is conserved across all eukaryotes. Retromer is most closely associated with the endosome-to-Golgi retrieval pathway and is necessary to maintain an active pool of hydrolase receptors in the trans-Golgi network. Recent progress in studies of retromer have identified new retromer-interacting proteins, including the WASH complex and cargo such as the Wntless/MIG-14 protein, which now extends the role of retromer beyond the endosome-to-Golgi pathway and has revealed that retromer is required for aspects of endosome-to-plasma membrane sorting and regulation of signalling events. The interactions between the retromer complex and other macromolecular protein complexes now show how endosomal protein sorting is coordinated with actin assembly and movement along microtubules, and place retromer squarely at the centre of a complex set of protein machinery that governs endosomal protein sorting. Dysregulation of retromer-mediated endosomal protein sorting leads to various pathologies, including neurodegenerative diseases such as Alzheimer disease and spastic paraplegia and the mechanisms underlying these pathologies are starting to be understood. In this Commentary, I will highlight recent advances in the understanding of retromer-mediated endosomal protein sorting and discuss how retromer contributes to a diverse set of physiological processes.

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“…In yeast, retromer is tightly associated with the sorting nexin (SNX) Vps5p/17p heterodimer, but, in other organisms, this link is more fragile (5)(6)(7)(8)(9). In Caenorhabditis elegans, the SNX-1/SNX-6 obligate heterodimer appears to function as the SNX complex most closely related to Vps5p/Vps17p (10,11).…”

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SNX-1 and RME-8 oppose the assembly of HGRS-1/ESCRT-0 degradative microdomains on endosomes

Norris

Tammineni

Wang

et al. 2017

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

100

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After endocytosis, transmembrane cargo reaches endosomes, where it encounters complexes dedicated to opposing functions: recycling and degradation. Microdomains containing endosomal sorting complexes required for transport (ESCRT)-0 component Hrs [hepatocyte growth factor-regulated tyrosine kinase substrate (HGRS-1) in Caenorhabditis elegans] mediate cargo degradation, concentrating ubiquitinated cargo and organizing the activities of ESCRT. At the same time, retromer associated sorting nexin one (SNX-1) and its binding partner, J-domain protein RME-8, sort cargo away from degradation, promoting cargo recycling to the Golgi. Thus, we hypothesized that there could be important regulatory interactions between retromer and ESCRT that balance degradative and recycling functions. Taking advantage of the naturally large endosomes of the C. elegans coelomocyte, we visualized complementary ESCRT-0 and RME-8/SNX-1 microdomains in vivo and assayed the ability of retromer and ESCRT microdomains to regulate one another. We found in snx-1(0) and rme-8(ts) mutants increased endosomal coverage and intensity of HGRS-1-labeled microdomains, as well as increased total levels of HGRS-1 bound to membranes. These effects are specific to SNX-1 and RME-8, as loss of other retromer components SNX-3 and vacuolar protein sorting-associated protein 35 (VPS-35) did not affect HGRS-1 microdomains. Additionally, knockdown of hgrs-1 had little to no effect on SNX-1 and RME-8 microdomains, suggesting directionality to the interaction. Separation of the functionally distinct ESCRT-0 and SNX-1/RME-8 microdomains was also compromised in the absence of RME-8 and SNX-1, a phenomenon we observed to be conserved, as depletion of Snx1 and Snx2 in HeLa cells also led to greater overlap of Rme-8 and Hrs on endosomes.endosome | SNX-1 | RME-8 | Hrs | clathrin

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Evolutionary variations of VPS29, and their implications for the heteropentameric model of retromer

Cited by 19 publications

References 11 publications

The giardial VPS35 retromer subunit is necessary for multimeric complex assembly and interaction with the vacuolar protein sorting receptor

The giardial VPS35 retromer subunit is necessary for multimeric complex assembly and interaction with the vacuolar protein sorting receptor

The retromer complex – endosomal protein recycling and beyond

SNX-1 and RME-8 oppose the assembly of HGRS-1/ESCRT-0 degradative microdomains on endosomes

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