High impact information on VPS26A

• VPS35 is the core molecule of the retromer trafficking complex and further analysis revealed that VPS26, another member of the complex, is also downregulated in AD [1].
• Identification and characterization of a novel, evolutionarily conserved gene disrupted by the murine H beta 58 embryonic lethal transgene insertion [2].
• The wild-type H beta 58 gene encodes a single 2.7 kb mRNA during embryonic and fetal development, and in many adult somatic tissues [2].
• 5. In this paper, we describe the characterization of a novel gene encoded at the H beta 58 locus, whose disruption appears to be responsible for the mutant phenotype [2].
• A similar change of memapsin 2 localization also was observed when a retromer subunit, VPS26, was depleted [3].

Biological context of VPS26A

• The open reading frame shows significant homology to Hbeta58, a mouse gene essential for embryogenesis, PEP8, a yeast homologue of Hbeta58, and an expressed sequence tag of Arabidopsis thariana, suggesting that DCRA has some important function that has been conserved during the course of evolution [4].

Anatomical context of VPS26A

• The loop is phylogenetically conserved and provides a mechanism for Vps26 integration into the complex that leaves the rest of the structure free for engagements with membranes and for conformational changes [5].

Associations of VPS26A with chemical compounds

• Hydrophobic residues and a glycine in this loop are required for integration into the retromer complex and endosomal localization of human Vps26, and for the function of yeast Vps26 in carboxypeptidase Y sorting [5].

Analytical, diagnostic and therapeutic context of VPS26A

• Sequence analysis of H beta 58 cDNA clones revealed no homology between the 38 x 10(3) M(r) H beta 58 protein and other known proteins [2].

References