| First Author | Tani K | Year | 1999 |
| Journal | J Biol Chem | Volume | 274 |
| Issue | 29 | Pages | 20505-12 |
| PubMed ID | 10400679 | Mgi Jnum | J:56260 |
| Mgi Id | MGI:1340708 | Doi | 10.1074/jbc.274.29.20505 |
| Citation | Tani K, et al. (1999) p125 is a novel mammalian Sec23p-interacting protein with structural similarity to phospholipid-modifying proteins. J Biol Chem 274(29):20505-12 |
| abstractText | COPII-coated vesicles are involved in protein transport from the endoplasmic reticulum to the Golgi apparatus. COPII consists of three parts: Sar1p and the two protein complexes, Sec23p-Sec24p and Sec13p-Sec31p. Using a glutathione S-transferase fusion protein with mouse Sec23p, we identified a novel mammalian Sec23p-interacting protein, p125, which is clearly distinct from Sec24p. The N-terminal region of p125 is rich in proline residues, and the central and C-terminal regions exhibit significant homology to phospholipid-modifying proteins, especially phosphatidic acid preferring-phospholipase A1. We transiently expressed p125 and mouse Sec23p in mammalian cells and examined their interaction. The results showed that the N-terminal region of p125 is important for the interaction with Sec23p. We confirmed the interaction between the two proteins by a yeast two-hybrid assay. Overexpression of p125, like that of mammalian Sec23p, caused disorganization of the endoplasmic reticulum-Golgi intermediate compartment and Golgi apparatus, suggesting its role in the early secretory pathway. |
