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Vacuolar protein sorting 26 homolog A

Vps26, PEP8, H beta 58, Vps26A
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. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: VPS35, Vps29, SNX1, ACID, IRBP
Papers using Vps26 antibodies
Dual specificity of the interfacial inhibitor brefeldin a for arf proteins and sec7 domains.
Caplan Steve H., In PLoS ONE, 2005
Covance), rabbit anti-HA(ICL), mouse anti-CD8 (Chemicon), rabbit anti-VPS26 (Abcam), mouse anti-CIMPR (BioLegend), mouse ...
Papers on Vps26
Structure of Spo0M, a sporulation-control protein from Bacillus subtilis.
Mikami et al., Uji, Japan. In Acta Crystallogr Sect F Struct Biol Commun, Jan 2016
In addition, Spo0M harbours a potential polar-core structure connecting the N- and C-terminal domains with several salt bridges, as seen in the crystal structures of arrestin and VPS26.
Vps26B-retromer negatively regulates plasma membrane resensitization of PAR-2.
Teasdale et al., Brisbane, Australia. In Cell Biol Int, Nov 2015
Retromer is a trimeric complex composed of Vps26, Vps29, and Vps35 and has been shown to be involved in trafficking and sorting of transmembrane proteins within the endosome.
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.
Conditional U1 Gene Silencing in Toxoplasma gondii.
Meissner et al., Glasgow, United Kingdom. In Plos One, 2014
Here we describe a simple method that combines endogenous tagging with DiCre-mediated positioning of U1 recognition sites adjacent to the termination codon of the GOI which leads to a conditional knockdown of the GOI upon rapamycin-induction. Specific knockdown mutants of the reporter gene GFP and several endogenous genes of T. gondii including the clathrin heavy chain gene 1 (chc1), the vacuolar protein sorting gene 26 (vps26), and the dynamin-related protein C gene (drpC) were silenced using this approach and demonstrate the potential of this technology.
A unique PDZ domain and arrestin-like fold interaction reveals mechanistic details of endocytic recycling by SNX27-retromer.
Cullen et al., Bristol, United Kingdom. In Proc Natl Acad Sci U S A, 2014
Crystal structures and NMR experiments reveal that an exposed β-hairpin in the SNX27 PDZ domain engages a groove in the arrestin-like structure of the vacuolar protein sorting 26A (VPS26A) retromer subunit.
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.
Hyperleucinemia causes hippocampal retromer deficiency linking diabetes to Alzheimer's disease.
Small et al., New York City, United States. In Neurobiol Dis, 2014
Retromer-dependent trafficking is implicated in the pathogenesis of AD, and two key retromer proteins, VPS35 and VPS26, are deficient in the hippocampal formation of AD patients.
The Vps35 D620N mutation linked to Parkinson's disease disrupts the cargo sorting function of retromer.
Teasdale et al., Australia. In Traffic, 2014
The retromer is a trimeric cargo-recognition protein complex composed of Vps26, Vps29 and Vps35 associated with protein trafficking within endosomes.
V-ATPase-dependent luminal acidification is required for endocytic recycling of a yeast cell wall stress sensor, Wsc1p.
Toshima et al., Tokyo, Japan. In Biochem Biophys Res Commun, 2014
Moreover, we found that deletion of the VPS26 gene, encoding a subunit of the retromer complex, also caused a defect in Wsc1p recycling and mis-localization of Wsc1p to the vacuole.
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.
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.
A global analysis of SNX27-retromer assembly and cargo specificity reveals a function in glucose and metal ion transport.
Cullen et al., Bristol, United Kingdom. In Nat Cell Biol, 2013
Furthermore, we establish that direct interaction of the SNX27 PDZ domain with the retromer subunit VPS26 is necessary and sufficient to prevent lysosomal entry of SNX27 cargo.
True arrestins and arrestin-fold proteins: a structure-based appraisal.
Klein et al., Grenoble, France. In Prog Mol Biol Transl Sci, 2012
In human, it includes the well-characterized visual and β-arrestins, the arrestin domain-containing proteins (ARRDCs), isoforms of the retromer subunit VPS26, and DSCR3, a protein involved in Down syndrome.
Rabankyrin-5 interacts with EHD1 and Vps26 to regulate endocytic trafficking and retromer function.
Caplan et al., Omaha, United States. In Traffic, 2012
Rabankyrin-5 interacts with EHD1 and Vps26 to regulate endocytic trafficking and retromer function
Vps26A and Vps26B subunits define distinct retromer complexes.
Teasdale et al., Brisbane, Australia. In Traffic, 2011
Colocalization of Vps26 paralogues with different endosomally located Rab proteins shows prolonged association of Vps26B-retromer with maturing endosomes relative to Vps26A-retromer.
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.
Identification of novel retromer complexes in the mouse testis.
Chang et al., South Korea. In Biochem Biophys Res Commun, 2008
These results revealed that the retromer complex could be formed from different Vps26 isoforms in a tissue-specific manner.
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
Human retromer consists of two smaller complexes: the cargo recognition VPS26-VPS29-VPS35 heterotrimer and a membrane-targeting heterodimer or homodimer of SNX1 and/or SNX2 (ref.
Use of embryonic stem cells to study mutations affecting postimplantation development in the mouse.
Lee et al., New York City, United States. In Ciba Found Symp, 1991
We have been studying two independently generated insertional mutations termed 413.d and H beta 58 that result in early postimplantation lethality.
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