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Vacuolar protein sorting 29 homolog

Vps29, Vps29p
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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: VPS35, Vps26, CAN, SNX1, OUT
Papers using Vps29 antibodies
Regulation of retromer recruitment to endosomes by sequential action of Rab5 and Rab7
Bonifacino Juan S. et al., In The Journal of Cell Biology, 2004
... The Vps29-YFP construct was generated by PCR amplification of human Vps29 (residues 1–182; the stop codon TAA at position 183 was mutated to TAT, encoding a tyrosine residue) and cloning into the EcoRI and BamHI sites of the pEYFP-N1 vector (BD Biosciences).
Papers on Vps29
Expression, purification and characterization of Plasmodium falciparum vacuolar protein sorting 29.
Bandyopadhyay et al., Calcutta, India. In Protein Expr Purif, Jan 2016
Plasmodium falciparum VPS29 (PfVPS29) is predicted to be a functional component in the assembly of the retromer complex; however, so far detailed characterization of PfVPS29 in its native form is not yet done.
VPS29-VPS35 intermediate of retromer is stable and may be involved in the retromer complex assembly process.
Hattori et al., Tokyo, Japan. In Febs Lett, Jul 2015
VPS35 works as the central subunit of retromer to recognize the cargos and binds with VPS29 and VPS26 via distinct domains.
Genetic variability of the retromer cargo recognition complex in parkinsonism.
Farrer et al., Vancouver, Canada. In Mov Disord, Apr 2015
METHODS: Mutation screening of the coding regions of the retromer cargo recognition complex genes (VPS26A/B, VPS29, and VPS35) was carried out in patients with PD (n = 396), atypical parkinsonism (n = 229), and in 368 controls.
The Orthology Clause in the Next Generation Sequencing Era: Novel Reference Genes Identified by RNA-seq in Humans Improve Normalization of Neonatal Equine Ovary RT-qPCR Data.
Steinborn et al., Vienna, Austria. In Plos One, 2014
The expression stability of eleven novel RGs (C1orf43, CHMP2A, EMC7, GPI, PSMB2, PSMB4, RAB7A, REEP5, SNRPD3, VCP and VPS29) was assessed by RT-qPCR in ovaries of seven neonatal fillies and compared to that of the expressed repetitive element ERE-B, two universal (OAZ1 and RPS29) and four traditional RGs (ACTB, GAPDH, UBB and B2M).
Myrosin cell development is regulated by endocytosis machinery and PIN1 polarity in leaf primordia of Arabidopsis thaliana.
Hara-Nishimura et al., Kyoto, Japan. In Plant Cell, 2014
By contrast, myrosin cell development was not affected by deficiencies of vacuolar trafficking factors, including the vacuolar sorting receptor VSR1 and the retromer components VPS29 and VPS35, suggesting that endocytic pathway rather than vacuolar trafficking pathway is important for myrosin cell development.
Genetic variation of the retromer subunits VPS26A/B-VPS29 in Parkinson's disease.
Ross et al., Jacksonville, United States. In Neurobiol Aging, 2014
In the present study we sequenced 702 affected subjects from the Mayo Clinic Parkinson's disease patient-control series for the VPS29 and VPS26A/B genes.
VARP is recruited on to endosomes by direct interaction with retromer, where together they function in export to the cell surface.
Owen et al., Cambridge, United Kingdom. In Dev Cell, 2014
We show that recruitment of VARP to the endosomal membrane is mediated by its direct interaction with VPS29, a subunit of the retromer complex, which is involved in trafficking from endosomes to the TGN and the cell surface.
RME-8 coordinates the activity of the WASH complex with the function of the retromer SNX dimer to control endosomal tubulation.
Seaman et al., Cambridge, United Kingdom. In J Cell Sci, 2014
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.
TBC1D5 and the AP2 complex regulate ATG9 trafficking and initiation of autophagy.
Dikic et al., Frankfurt am Main, Germany. In Embo Rep, 2014
The RabGAP protein TBC1D5 controls cellular endomembrane trafficking processes and binds the retromer subunit VPS29 and the ubiquitin-like protein ATG8 (LC3).
A mechanism for retromer endosomal coat complex assembly with cargo.
Burd et al., New Haven, United States. In Proc Natl Acad Sci U S A, 2014
Retromer is an evolutionarily conserved protein complex composed of the VPS26, VPS29, and VPS35 proteins that selects and packages cargo proteins into transport carriers that export cargo from the endosome.
The giardial VPS35 retromer subunit is necessary for multimeric complex assembly and interaction with the vacuolar protein sorting receptor.
Touz et al., Córdoba, Argentina. In Biochim Biophys Acta, 2013
Homologs of the retromer Vacuolar Protein Sorting (Vps35p, Vps26p, and Vps29p) have been identified in this parasite.
Retromer association with membranes: plants have their own rules!
Gaude et al., Lyon, France. In Plant Signal Behav, 2013
We characterized Arabidopsis vps26 null mutant and showed that it displays severe developmental defaults similar to those observed in vps29 mutant.
Implication of mouse Vps26b-Vps29-Vps35 retromer complex in sortilin trafficking.
Chang et al., South Korea. In Biochem Biophys Res Commun, 2011
These results suggest that mouse Vps26b-Vps29-Vps35 retromer complex is implicated in the transport of sortilin from endosomes to the trans-Golgi network.
VPS29 is not an active metallo-phosphatase but is a rigid scaffold required for retromer interaction with accessory proteins.
Collins et al., Australia. In Plos One, 2010
Conclusion is that VPS29 is a metal ion-independent, rigid scaffolding domain, which is essential but not sufficient for incorporation of retromer into functional endosomal transport assemblies.
Retromer recycles vacuolar sorting receptors from the trans-Golgi network.
Pimpl et al., Heidelberg, Germany. In Plant J, 2010
A combination of immunoelectron and fluorescence microscopy show that VPS29p localize to the trans-Golgi network (TGN), which is considered to represent the early endosome of plants.
Membrane recruitment of the cargo-selective retromer subcomplex is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5.
Bright et al., Cambridge, United Kingdom. In J Cell Sci, 2009
Membrane recruitment of the cargo-selective retromer subcomplex VPS35/29/26 is catalysed by the small GTPase Rab7 and inhibited by the Rab-GAP TBC1D5.
Structural features of vps35p involved in interaction with other subunits of the retromer complex.
Nothwehr et al., Columbia, United States. In Traffic, 2007
the R(98) residue, which is part of a conserved PRLYL motif, is critical for Vps35p binding to Vps26p, while both R(98) and residues 733-944 are needed for efficient binding to Vps29p
Functional architecture of the retromer cargo-recognition complex.
Hurley et al., Bethesda, United States. In Nature, 2007
crystal structure of a VPS29-VPS35 subcomplex showing how the metallophosphoesterase-fold subunit VPS29 acts as a scaffold for the carboxy-terminal half of VPS35
The retromer protein VPS29 links cell polarity and organ initiation in plants.
Gaude et al., Lyon, France. In Cell, 2007
VPS29 is required for endosome homeostasis, PIN protein cycling, and dynamic PIN1 repolarization during plant organ development.
The mammalian retromer regulates transcytosis of the polymeric immunoglobulin receptor.
Mostov et al., San Francisco, United States. In Nat Cell Biol, 2004
The other is the Vps35p-Vps29p-Vps26p subcomplex, which provides cargo specificity.
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