| First Author | Bielli A | Year | 2001 |
| Journal | Biochem Biophys Res Commun | Volume | 281 |
| Issue | 5 | Pages | 1141-53 |
| PubMed ID | 11243854 | Mgi Jnum | J:68119 |
| Mgi Id | MGI:1932159 | Doi | 10.1006/bbrc.2001.4468 |
| Citation | Bielli A, et al. (2001) The small gtpase rab4a interacts with the central region of cytoplasmic dynein light intermediate chain-1. Biochem Biophys Res Commun 281(5):1141-53 |
| abstractText | Rab4 belongs to the Rab family of small GTPases involved in the regulation of intracellular transport, and has been localized to early endosomes. We have employed the yeast two-hybrid system to identify proteins that specifically interact with Rab4AQ67L, a GTPase-deficient mutant form of Rab4A. Screening a mouse embryo cDNA library identified a clone (M449) that interacted with Rab4A in a nucleotide-dependent fashion. Data base searches identified this clone as the mouse cytoplasmic dynein light intermediate chain-1 (LIC-1). Based on this finding, the full-length equivalent human cytoplasmic dynein LIC-1 was isolated by PCR. When Rab4A was overexpressed together with either M449 or dynein LIC-1 in HeLa cells, the proteins were found to colocalize in the perinuclear region. We characterize the localization of both overexpressed human dynein LIC-1 and the endogenous protein with respect to microtubules and show that it concentrates to the microtubule-organizing center and mitotic spindle. Additionally, GFPRab4A endosomes localize to microtubules and are redistributed by nocodazole treatment. This is the first described interaction between cytoplasmic dynein, a retrograde motor protein, and a Rab protein. Copyright 2001 Academic Press. |
