| First Author | Pooley RD | Year | 2008 |
| Journal | J Cell Sci | Volume | 121 |
| Issue | Pt 20 | Pages | 3413-21 |
| PubMed ID | 18827011 | Mgi Jnum | J:140958 |
| Mgi Id | MGI:3814962 | Doi | 10.1242/jcs.032847 |
| Citation | Pooley RD, et al. (2008) Murine CENPF interacts with syntaxin 4 in the regulation of vesicular transport. J Cell Sci 121(Pt 20):3413-21 |
| abstractText | Syntaxin 4 is a component of the SNARE complex that regulates membrane docking and fusion. Using a yeast two-hybrid screen, we identify a novel interaction between syntaxin 4 and cytoplasmic murine CENPF, a protein previously demonstrated to associate with the microtubule network and SNAP-25. The binding domain for syntaxin 4 in CENPF was defined by yeast two-hybrid assay and co-immunoprecipitation. Confocal analyses in cell culture reveal a high degree of colocalization between endogenously expressed proteins in interphase cells. Additionally, the endogenous SNARE proteins can be isolated as a complex with CENPF in immunoprecipitation experiments. Further analyses demonstrate that murine CENPF and syntaxin 4 colocalize with components of plasma membrane recycling: SNAP-25 and VAMP2. Depletion of endogenous CENPF disrupts GLUT4 trafficking whereas expression of a dominant-negative form of CENPF inhibits cell coupling. Taken together, these studies demonstrate that CENPF provides a direct link between proteins of the SNARE system and the microtubule network and indicate a diverse role for murine CENPF in vesicular transport. |
