| First Author | Scherer PE | Year | 1996 |
| Journal | J Cell Biol | Volume | 133 |
| Issue | 2 | Pages | 257-68 |
| PubMed ID | 8609160 | Mgi Jnum | J:32511 |
| Mgi Id | MGI:80005 | Doi | 10.1083/jcb.133.2.257 |
| Citation | Scherer PE, et al. (1996) Cab45, a novel (Ca2+)-binding protein localized to the Golgi lumen. J Cell Biol 133(2):257-68 |
| abstractText | We have identified and characterized Cab45, a novel 45-kD protein from mouse 3T3-L1 adipocytes. Cab45 is ubiquitously expressed, contains an NH2-terminal signal sequence but no membrane-anchor sequences, and binds Ca2+ due to the presence of six EF-hand motifs. Within the superfamily of calcium-binding proteins, it belongs to a recently identified group of proteins consisting of Reticulocalbin (Ozawa, M., and T. Muramatsu. 1993. J. Biol. Chem. 268:699-705) and ERC 55 (Weis, K., G. Griffiths, and A.I. Lamond. 1994. J. Biol Chem. 269:19142-19150), both of which share significant sequence homology with Cab45 outside the EF-hand motifs. In contrast to reticulocalbin and ERC-55 which are soluble components of the endoplasmic reticulum, Cab45 is a soluble protein localized to the Golgi. Cab45 is the first calcium-binding protein localized to the lumenal portion of a post-ER compartment; Cab45 is also the first known soluble protein resident in the Golgi lumen. Cab45 can serve as a model protein to determine the mechanism of retention of soluble proteins in the Golgi compartment. |
