VPS35

VPS35
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2R17
Identifiers
Aliases	VPS35, MEM3, PARK17, VPS35 retromer complex component, retromer complex component
External IDs	MGI: 1890467 HomoloGene: 6221 GeneCards: VPS35
Gene location (Human)
Chr.	Chromosome 16 (human)[1]
End	46,689,518 bp[1]
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)[2]
End	85,299,802 bp[2]
RNA expression pattern
	More reference expression data
Gene ontology
Molecular function	• protein binding; • D1 dopamine receptor binding; • protein transporter activity;
Cellular component	• cytoplasm; • endosome; • membrane; • tubular endosome; • retromer complex; • lysosomal membrane; • early endosome; • extracellular exosome; • mitochondrion; • lysosome; • endosome membrane; • postsynaptic density; • retromer, cargo-selective complex; • mitochondrion-derived vesicle; • neuron projection; • neuronal cell body; • perinuclear region of cytoplasm; • late endosome; • cytosol;
Biological process	• regulation of protein stability; • positive regulation of canonical Wnt signaling pathway; • positive regulation of Wnt protein secretion; • transcytosis; • negative regulation of late endosome to lysosome transport; • retrograde transport, endosome to Golgi; • protein transport; • retrograde transport, endosome to plasma membrane; • regulation of macroautophagy; • Wnt signaling pathway; • regulation of mitochondrion organization; • mitochondrial fragmentation involved in apoptotic process; • positive regulation of dopamine receptor signaling pathway; • positive regulation of mitochondrial fission; • mitochondrion to lysosome transport; • neurotransmitter receptor transport, endosome to plasma membrane; • regulation of dendritic spine maintenance; • GO:2000600 positive regulation of cellular protein catabolic process; • regulation of terminal button organization; • lysosome organization; • positive regulation of gene expression; • negative regulation of gene expression; • protein destabilization; • negative regulation of protein homooligomerization; • protein localization to organelle; • voluntary musculoskeletal movement; • positive regulation of locomotion involved in locomotory behavior; • positive regulation of dopamine biosynthetic process; • negative regulation of cellular protein localization; • negative regulation of lysosomal protein catabolic process; • transport; • regulation of cellular protein metabolic process; • negative regulation of inflammatory response; • negative regulation of cell death; • negative regulation of neuron death; • regulation of presynapse assembly;
	Sources:Amigo / QuickGO
Orthologs
	55737
	65114
	ENSG00000069329
	ENSMUSG00000031696
	Q96QK1
	Q9EQH3
	NM_018206
	NM_022997
	NP_060676
	NP_075373
	Wikidata
View/Edit Human	View/Edit Mouse

Vacuolar protein sorting-associated protein 35 is a protein that in humans is encoded by the VPS35 gene.^[5]^[6]

This gene belongs to a group of vacuolar protein sorting (VPS) genes. The encoded protein is a component of a large multimeric complex, termed the retromer complex, involved in retrograde transport of proteins from endosomes to the trans-Golgi network. The close structural similarity between the yeast and human proteins that make up this complex suggests a similarity in function. Expression studies in yeast and mammalian cells indicate that this protein interacts directly with VPS35, which serves as the core of the retromer complex.^[6]

Structure

Vps35 is the largest subunit of retromer with the molecular weight of 92-kDa and functions as the central platform for the assembly of Vps26 and Vps29.^[7] Vps35 resembles many other helical solenoid proteins including AP adaptor protein complexes that are characterized with repeated structural units in a continuous superhelix arrangement involved in coated vesicle trafficking. The curved surface of the 6 even-numbered helices within solenoid structure with series of ridges separating hydrophobic grooves function as potential cargo binding sites.^[8] The C-terminal of Vps35 contains an α-solenoid fold that fits into the metal binding pocket of Vps29.^[9]

A conserved PRLYL motif at the N-terminus of Vps35 is involved in the binding of Vps26.^[10]^[11] The structural binding motifs enable this subunit to act as a linker between the SNX dimers and Vps trimer complex, and the binding sites targeting to the N-terminal region of SNX subunits are located at the both ends of the trimer. A study has shown that the knockdown of Vps35 in human HEp-2 epithelial cells had defect on the endosomal recycling of transferrin by DMT1 due to the mis-sorting of DMT1-II to the lysosomal membrane associated protein (LAMP2) structures.^[12]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000069329 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031696 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Zhang P, Yu L, Gao J, Fu Q, Dai F, Zhao Y, Zheng L, Zhao S (Jan 2001). "Cloning and characterization of human VPS35 and mouse Vps35 and mapping of VPS35 to human chromosome 16q13-q21". Genomics. 70 (2): 253–7. doi:10.1006/geno.2000.6380. PMID 11112353.
1 2 "Entrez Gene: VPS35 vacuolar protein sorting 35 homolog (S. cerevisiae)".
↑ Hierro A, Rojas AL, Rojas R, Murthy N, Effantin G, Kajava AV, Steven AC, Bonifacino JS, Hurley JH (October 2007). "Functional architecture of the retromer cargo-recognition complex". Nature. 449 (7165): 1063–7. doi:10.1038/nature06216. PMC 2377034. PMID 17891154.
↑ Nothwehr SF, Bruinsma P, Strawn LA (April 1999). "Distinct domains within Vps35p mediate the retrieval of two different cargo proteins from the yeast prevacuolar/endosomal compartment". Mol. Biol. Cell. 10 (4): 875–90. doi:10.1091/mbc.10.4.875. PMC 25208. PMID 10198044.
↑ Collins BM, Skinner CF, Watson PJ, Seaman MN, Owen DJ (July 2005). "Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly". Nat. Struct. Mol. Biol. 12 (7): 594–602. doi:10.1038/nsmb954. PMID 15965486.
↑ Reddy JV, Seaman MN (October 2001). "Vps26p, a component of retromer, directs the interactions of Vps35p in endosome-to-Golgi retrieval". Mol. Biol. Cell. 12 (10): 3242–56. doi:10.1091/mbc.12.10.3242. PMC 60170. PMID 11598206.
↑ Zhao X, Nothwehr S, Lara-Lemus R, Zhang BY, Peter H, Arvan P (December 2007). "Dominant-negative behavior of mammalian Vps35 in yeast requires a conserved PRLYL motif involved in retromer assembly". Traffic. 8 (12): 1829–40. doi:10.1111/j.1600-0854.2007.00658.x. PMC 2532708. PMID 17916227.
↑ Tabuchi M, Yanatori I, Kawai Y, Kishi F (March 2010). "Retromer-mediated direct sorting is required for proper endosomal recycling of the mammalian iron transporter DMT1". J. Cell Sci. 123 (Pt 5): 756–66. doi:10.1242/jcs.060574. PMID 20164305.

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA (1997). "Large-Scale Concatenation cDNA Sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Edgar AJ, Polak JM (2000). "Human homologues of yeast vacuolar protein sorting 29 and 35". Biochem. Biophys. Res. Commun. 277 (3): 622–30. doi:10.1006/bbrc.2000.3727. PMID 11062004.
Hartley JL, Temple GF, Brasch MA (2001). "DNA Cloning Using In Vitro Site-Specific Recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Haft CR, de la Luz Sierra M, Bafford R, Lesniak MA, Barr VA, Taylor SI (2001). "Human Orthologs of Yeast Vacuolar Protein Sorting Proteins Vps26, 29, and 35: Assembly into Multimeric Complexes". Mol. Biol. Cell. 11 (12): 4105–16. doi:10.1091/mbc.11.12.4105. PMC 15060. PMID 11102511.
Vergés M, Luton F, Gruber C, Tiemann F, Reinders LG, Huang L, Burlingame AL, Haft CR, Mostov KE (2004). "The mammalian retromer regulates transcytosis of the polymeric immunoglobulin receptor". Nat. Cell Biol. 6 (8): 763–9. doi:10.1038/ncb1153. PMID 15247922.
Mingot JM, Bohnsack MT, Jäkle U, Görlich D (2005). "Exportin 7 defines a novel general nuclear export pathway". EMBO J. 23 (16): 3227–36. doi:10.1038/sj.emboj.7600338. PMC 514512. PMID 15282546.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000069329 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031696 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid11112353-5] Zhang P, Yu L, Gao J, Fu Q, Dai F, Zhao Y, Zheng L, Zhao S (Jan 2001). "Cloning and characterization of human VPS35 and mouse Vps35 and mapping of VPS35 to human chromosome 16q13-q21". Genomics. 70 (2): 253–7. doi:10.1006/geno.2000.6380. PMID 11112353.

[entrez-6] 1 2 "Entrez Gene: VPS35 vacuolar protein sorting 35 homolog (S. cerevisiae)".

[pmid17891154-7] Hierro A, Rojas AL, Rojas R, Murthy N, Effantin G, Kajava AV, Steven AC, Bonifacino JS, Hurley JH (October 2007). "Functional architecture of the retromer cargo-recognition complex". Nature. 449 (7165): 1063–7. doi:10.1038/nature06216. PMC 2377034. PMID 17891154.

[pmid10198044-8] Nothwehr SF, Bruinsma P, Strawn LA (April 1999). "Distinct domains within Vps35p mediate the retrieval of two different cargo proteins from the yeast prevacuolar/endosomal compartment". Mol. Biol. Cell. 10 (4): 875–90. doi:10.1091/mbc.10.4.875. PMC 25208. PMID 10198044.

[pmid15965486-9] Collins BM, Skinner CF, Watson PJ, Seaman MN, Owen DJ (July 2005). "Vps29 has a phosphoesterase fold that acts as a protein interaction scaffold for retromer assembly". Nat. Struct. Mol. Biol. 12 (7): 594–602. doi:10.1038/nsmb954. PMID 15965486.

[pmid11598206-10] Reddy JV, Seaman MN (October 2001). "Vps26p, a component of retromer, directs the interactions of Vps35p in endosome-to-Golgi retrieval". Mol. Biol. Cell. 12 (10): 3242–56. doi:10.1091/mbc.12.10.3242. PMC 60170. PMID 11598206.

[pmid17916227-11] Zhao X, Nothwehr S, Lara-Lemus R, Zhang BY, Peter H, Arvan P (December 2007). "Dominant-negative behavior of mammalian Vps35 in yeast requires a conserved PRLYL motif involved in retromer assembly". Traffic. 8 (12): 1829–40. doi:10.1111/j.1600-0854.2007.00658.x. PMC 2532708. PMID 17916227.

[pmid20164305-12] Tabuchi M, Yanatori I, Kawai Y, Kishi F (March 2010). "Retromer-mediated direct sorting is required for proper endosomal recycling of the mammalian iron transporter DMT1". J. Cell Sci. 123 (Pt 5): 756–66. doi:10.1242/jcs.060574. PMID 20164305.

VPS35

Structure

References

Further reading