The small GTPase Rab4A interacts with the central region of cytoplasmic dynein light intermediate chain-1.

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.
Mesh Terms:
Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, Cytoplasmic Dyneins, Dyneins, Endosomes, HL-60 Cells, Hela Cells, Humans, Jurkat Cells, Mice, Microtubule-Organizing Center, Microtubules, Mitotic Spindle Apparatus, Molecular Sequence Data, Mutation, Nocodazole, Sequence Homology, Amino Acid, Two-Hybrid System Techniques, rab4 GTP-Binding Proteins
Biochem. Biophys. Res. Commun.
Date: Mar. 01, 2001
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