| First Author | Bascom RA | Year | 1999 |
| Journal | J Biol Chem | Volume | 274 |
| Issue | 5 | Pages | 2953-62 |
| PubMed ID | 9915833 | Mgi Jnum | J:52425 |
| Mgi Id | MGI:1329272 | Doi | 10.1074/jbc.274.5.2953 |
| Citation | Bascom RA, et al. (1999) Identification and characterization of golgin-84, a novel Golgi integral membrane protein a cyto-plasmic coiled-coil domain [published erratum appears in J Biol Chem 1999 Apr 30;274(18):12950]. J Biol Chem 274(5):2953-62 |
| abstractText | The cytoplasmic face of the Golgi contains a variety of proteins with coiled-coil domains. We identified one such protein in a yeast two-hybrid screen, using as bait the peripheral Golgi phosphatidylinositol(4,5)P2 5-phosphatase OCRL1 that is implicated in a human disease, the oculocerebrorenal syndrome. The approximately 2.8-kilobase mRNA is ubiquitously expressed and abundant in testis; it encodes a 731-amino acid protein with a predicted mass of 83 kDa. Antibodies against the sequence detect a novel approximately 84-kDa Golgi protein we termed golgin-84. Golgin-84 is an integral membrane protein with a single transmembrane domain close to its C terminus. In vitro, the protein inserts post-translationally into microsomal membranes with an N-cytoplasmic and C-lumen orientation. Cross-linking indicates that golgin-84 forms dimers, consistent with the prediction of an approximately 400-residue dimerizing coiled-coil domain in its N terminus. The dimerization potential is supported by a data base search that showed that the N-terminal 497 residues of golgin-84 contain a coiled-coil domain that when fused to the RET tyrosine kinase domain had the ability to activate it, forming the RET-II oncogene. Data base searching also indicates golgin-84 is similar in structure and sequence to giantin, a membrane protein that tethers coatamer complex I vesicles to the Golgi. |
