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VPS26A belongs to a group of vacuolar protein sorting (VPS) genes. Additionally we are shipping Vacuolar Protein Sorting 26 Homolog A (S. Pombe) Antibodies (50) and many more products for this protein.
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X-ray crystallographic analysis of a 4-component complex comprising the VPS26 & VPS35 (show vps35 Proteins) subunits of retromer, sorting nexin SNX3 (show SNX3 Proteins), & recycling signal from the divalent cation transporter DMT1 (show DMRT1 Proteins)-II; analysis identifies a binding site for canonical recycling signals at the interface between VPS26 & SNX3 (show SNX3 Proteins); shows cooperative interactions among the VPS subunits, SNX3 (show SNX3 Proteins) & cargo that couple signal-recognition to membrane recruitment.
Mutagenesis studies coupled with coimmunoprecipitations revealed that retromer-mediated trafficking requires the Env cytoplasmic tail that we show binds directly to retromer components Vps35 and Vps26.
provides molecular insights into the essential role of Vps26 and Vps35 (show vps35 Proteins) in Rab7 (show RAB7B Proteins)-mediated recruitment of the core retromer complex
This study demonstrated that Genetic variability of VPS26A in parkinsonism.
Mutations in VPS26A are not a frequent cause of Parkinson's disease.
VPS26A binding increases the affinity of the SNX27 PDZ domain for PDZ- binding motifs by an order of magnitude, revealing cooperativity in cargo selection.
Rabankyrin-5 interacts with EHD1 and Vps26 to regulate endocytic trafficking and retromer function
Colocalization of Vps26 paralogues with different endosomally located Rab (show HRB Proteins) proteins shows prolonged association of Vps26B (show VPS26B Proteins)-retromer with maturing endosomes relative to Vps26A-retromer.
These observations indicate that the mammalian retromer complex assembles by sequential association of SNX1 (show SNX1 Proteins)/2 and Vps26-Vps29 (show VPS29 Proteins)-Vps35 (show vps35 Proteins) subcomplexes on endosomal membranes and that SNX1 (show SNX1 Proteins) and SNX2 (show SNX2 Proteins) play interchangeable but essential roles.
Membrane recruitment of the cargo-selective retromer subcomplex VPS35 (show vps35 Proteins)/29/26 is catalysed by the small GTPase (show RACGAP1 Proteins) Rab7 (show RAB7B Proteins) and inhibited by the Rab (show HRB Proteins)-GAP TBC1D5 (show TBC1D5 Proteins).
Vps26 is implicated in regulating Vps35p membrane association, therefore Vps26 plays a role in cargo recognition of the cytoplasmic coat retromer complex.
These results revealed that the retromer complex could be formed from different Vps26 isoforms in a tissue-specific manner.
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.
vacuolar protein sorting 26 homolog A (S. pombe)
, vacuolar protein sorting-associated protein 26A
, vacuolar protein sorting-associated protein 26A-like
, vacuolar protein sorting 26 A
, vacuolar protein sorting 26
, vacuolar protein sorting homolog26
, Zea mouse H58 homolog1
, vesicle protein sorting 26A
, H beta 58
, vacuole protein sorting 26
, h58 protein