VPS29

Vacuolar protein sorting 29 homolog (S. cerevisiae), also known as VPS29, is a human gene.cite web | title = Entrez Gene: VPS29 vacuolar protein sorting 29 homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51699| accessdate = ]

This gene belongs to a group of vacuolar protein sorting (VPS) genes that, when functionally impaired, disrupt the efficient delivery of vacuolar hydrolases. The protein encoded by this gene is a component of a large multimeric complex, termed the retromer complex, which is involved in retrograde transport of proteins from endosomes to the trans-Golgi network. This VPS protein may be involved in the formation of the inner shell of the retromer coat for retrograde vesicles leaving the prevacuolar compartment. Alternative splice variants encoding different isoforms, and usage of multiple polyadenylation sites have been found for this gene.cite web | title = Entrez Gene: VPS29 vacuolar protein sorting 29 homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51699| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Seaman MN, McCaffery JM, Emr SD |title=A membrane coat complex essential for endosome-to-Golgi retrograde transport in yeast. |journal=J. Cell Biol. |volume=142 |issue= 3 |pages= 665–81 |year= 1998 |pmid= 9700157 |doi=
*cite journal | author=Edgar AJ, Polak JM |title=Human homologues of yeast vacuolar protein sorting 29 and 35. |journal=Biochem. Biophys. Res. Commun. |volume=277 |issue= 3 |pages= 622–30 |year= 2000 |pmid= 11062004 |doi= 10.1006/bbrc.2000.3727
*cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=
*cite journal | author=Haft CR, de la Luz Sierra M, Bafford R, "et al." |title=Human orthologs of yeast vacuolar protein sorting proteins Vps26, 29, and 35: assembly into multimeric complexes. |journal=Mol. Biol. Cell |volume=11 |issue= 12 |pages= 4105–16 |year= 2001 |pmid= 11102511 |doi=
*cite journal | author=Wiemann S, Weil B, Wellenreuther R, "et al." |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422–35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701
*cite journal | author=Simpson JC, Wellenreuther R, Poustka A, "et al." |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287–92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Vergés M, Luton F, Gruber C, "et al." |title=The mammalian retromer regulates transcytosis of the polymeric immunoglobulin receptor. |journal=Nat. Cell Biol. |volume=6 |issue= 8 |pages= 763–9 |year= 2004 |pmid= 15247922 |doi= 10.1038/ncb1153
*cite journal | author=Mingot JM, Bohnsack MT, Jäkle U, Görlich D |title=Exportin 7 defines a novel general nuclear export pathway. |journal=EMBO J. |volume=23 |issue= 16 |pages= 3227–36 |year= 2005 |pmid= 15282546 |doi= 10.1038/sj.emboj.7600338
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Wiemann S, Arlt D, Huber W, "et al." |title=From ORFeome to biology: a functional genomics pipeline. |journal=Genome Res. |volume=14 |issue= 10B |pages= 2136–44 |year= 2004 |pmid= 15489336 |doi= 10.1101/gr.2576704
*cite journal | author=Wang D, Guo M, Liang Z, "et al." |title=Crystal structure of human vacuolar protein sorting protein 29 reveals a phosphodiesterase/nuclease-like fold and two protein-protein interaction sites. |journal=J. Biol. Chem. |volume=280 |issue= 24 |pages= 22962–7 |year= 2005 |pmid= 15788412 |doi= 10.1074/jbc.M500464200
*cite journal | author=Mehrle A, Rosenfelder H, Schupp I, "et al." |title=The LIFEdb database in 2006. |journal=Nucleic Acids Res. |volume=34 |issue= Database issue |pages= D415–8 |year= 2006 |pmid= 16381901 |doi= 10.1093/nar/gkj139
*cite journal | author=Damen E, Krieger E, Nielsen JE, "et al." |title=The human Vps29 retromer component is a metallo-phosphoesterase for a cation-independent mannose 6-phosphate receptor substrate peptide. |journal=Biochem. J. |volume=398 |issue= 3 |pages= 399–409 |year= 2006 |pmid= 16737443 |doi= 10.1042/BJ20060033
*cite journal | author=Rojas R, Kametaka S, Haft CR, Bonifacino JS |title=Interchangeable but essential functions of SNX1 and SNX2 in the association of retromer with endosomes and the trafficking of mannose 6-phosphate receptors. |journal=Mol. Cell. Biol. |volume=27 |issue= 3 |pages= 1112–24 |year= 2007 |pmid= 17101778 |doi= 10.1128/MCB.00156-06
*cite journal | author=Hierro A, Rojas AL, Rojas R, "et al." |title=Functional architecture of the retromer cargo-recognition complex. |journal=Nature |volume=449 |issue= 7165 |pages= 1063–7 |year= 2007 |pmid= 17891154 |doi= 10.1038/nature06216

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