| First Author | Pooley RD | Year | 2006 |
| Journal | Mol Biol Cell | Volume | 17 |
| Issue | 7 | Pages | 3176-86 |
| PubMed ID | 16672379 | Mgi Jnum | J:112723 |
| Mgi Id | MGI:3663229 | Doi | 10.1091/mbc.E05-12-1127 |
| Citation | Pooley RD, et al. (2006) CytLEK1 is a regulator of plasma membrane recycling through its interaction with SNAP-25. Mol Biol Cell 17(7):3176-86 |
| abstractText | SNAP-25 is a component of the SNARE complex that is involved in membrane docking and fusion. Using a yeast two-hybrid screen, we identify a novel interaction between SNAP-25 and cytoplasmic Lek1 (cytLEK1), a protein previously demonstrated to associate with the microtubule network. The binding domains within each protein were defined by yeast two-hybrid, coimmunoprecipitation, and colocalization studies. Confocal analyses reveal a high degree of colocalization between the proteins. In addition, the endogenous proteins can be isolated as a complex by immunoprecipitation. Further analyses demonstrate that cytLEK1 and SNAP-25 colocalize and coprecipitate with Rab11a, myosin Vb, VAMP2, and syntaxin 4, components of the plasma membrane recycling pathway. Overexpression of the SNAP-25-binding domain of cytLEK1, and depletion of endogenous Lek1 alters transferrin trafficking, consistent with a function in vesicle recycling. Taken together, our studies indicate that cytLEK1 is a link between recycling vesicles and the microtubule network through its association with SNAP-25. This interaction may play a key role in the regulation of the recycling endosome pathway. |
