Rabbit Anti-Human VPS54 Polyclonal antibody

A novel gene, VPS54-like (Vps54l), is described in the rat that is homologous to the yeast Vps54 gene which is known to be involved in intracellular protein sorting. Furthermore, Vps54-related sequences of human, mouse, Drosophila melanogaster, Caenorhabditis elegans and Arabidopsis thaliana could be identified in the EMBL/GenBank/DDBJ database. Each of the deduced amino acid sequences of the VpS54 genes in these species contain a coiled-coil region and eight to 13 dileucine motifs. The rat Vps54l gene could be mapped to the end of chromosome 14 by radiation hybrid analysis 7 cR(3000) from the D14Rat22 marker and to 14q22 by fluorescence in situ hybridization. Using a rat Vps54l-containing P1-derived artificial chromosome (PAC) clone the respective ortholog was mapped to chromosome 11A3 in the mouse. In addition, the rat genome contains, a processed pseudogene of Vps54l on chromosome 7q22. PAC clone analysis shows that the rat Vps54l gene maps close to the UDP-glucose-pyrophosphorylase 2 gene. The two genes are in tail to tail orientation with their polyadenylation sites 497 bp apart. Rat Vps54l appears to be expressed ubiquitously, but at a relatively low level. Alternatively spliced transcripts could be isolated which lack the sequence coding for the coiled-coil region. (C) 2002 Elsevier Science B.V. All rights reserved.

Tethering factors are large protein complexes that capture transport vesicles and enable their fusion with acceptor organelles at different stages of the endomembrane system. Recent studies have shed new light on the structure and function of a heterotetrameric tethering factor named Golgi-associated retrograde protein (GARP), which promotes fusion of endosome-derived, retrograde transport carriers to the trans-Golgi network (TGN). X-ray crystallography of the Vps53 and Vps54 subunits of GARP has revealed that this complex is structurally related to other tethering factors such as the exocyst, the conserved oligomeric Golgi (COG) and Dsl1 (dependence on SLY1-20) complexes, indicating that they all might work by a similar mechanism. Loss of GARP function compromises the growth, fertility and/or viability of the defective organisms, emphasizing the essential nature of GARP-mediated retrograde transport.