| First Author | Nishimura Y | Year | 1999 |
| Journal | Biochem Biophys Res Commun | Volume | 254 |
| Issue | 1 | Pages | 21-6 |
| PubMed ID | 9920726 | Mgi Jnum | J:52046 |
| Mgi Id | MGI:1327742 | Doi | 10.1006/bbrc.1998.9876 |
| Citation | Nishimura Y, et al. (1999) Molecular cloning and characterization of mammalian homologues of vesicle-associated membrane protein-associated (VAMP-associated) proteins. Biochem Biophys Res Commun 254(1):21-6 |
| abstractText | We have identified human and rat homologues of the VAMP-associated protein (VAP) of 33 kDa of Aplysia californica (aVAP-33), which we designated VAP-A, VAP-B, and VAP-C. Human VAP-A (hVAP-A) was found to be identical to the recently reported protein hVAP-33, with the exception of two amino acid residues. VAP-B contained a coiled-coil domain and a transmembrane domain (TMD). Human VAP-B (hVAP-B) was 46 and 60% homologous of the amino acid level to aVAP-33 and hVAP-A, respectively. Human VAP-C was a splicing variant of hVAP-B, lacking both the coiled-coil domain and the TMD. hVAP-B had VAMP-binding ability. Moreover, hVAP-A and hVAP-B associated with each other through their respective TMDs. These results suggest that complex formation by VAPs might be important in the trafficking of mammalian vesicle. Copyright 1999 Academic Press. |
