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J Biol Chem, Vol. 273, Issue 46, 30065-30068, November 13, 1998

COMMUNICATION
Interaction of Doc2 with tctex-1, a Light Chain of Cytoplasmic Dynein
IMPLICATION IN DYNEIN-DEPENDENT VESICLE TRANSPORT

Fumiko Nagano, Satoshi Orita^§, Takuya Sasaki, Akira Naito^§, Gaku Sakaguchi^§, Miki Maeda^§, Tsuyoshi Watanabe^¶, Eiki Kominami, Yasuo Uchiyama^¶, and Yoshimi Takai

From the  Department of Molecular Biology and Biochemistry, the ^¶ Department of Cell Biology and Anatomy I, Osaka University Medical School, Suita 565-0871, the ^§ Shionogi Institute for Medical Science, Settsu 566-0022, and the  Department of Biochemistry, Juntendo University School of Medicine, Tokyo 113-0033, Japan

Doc2 has one Munc13-interacting domain at the N-terminal region and two C2-like domains interacting with Ca²⁺ and phospholipid at the C-terminal region. Doc2 consists of two isoforms, Doc2 and -. Doc2 is specifically expressed in neuronal cells and implicated in Ca²⁺-dependent neurotransmitter release, whereas Doc2 is ubiquitously expressed and its function is unknown. We show here that both Doc2 and - interact with rat tctex-1, a light chain of cytoplasmic dynein, in both cell-free and intact cell systems. Overexpression of the N-terminal fragment of Doc2 containing the tctex-1-interacting domain induces changes in the intracellular localization of cation-independent mannose 6-phosphate receptor and its ligand, cathepsin D, which are transported from trans-Golgi network to late endosomes. Overexpression of the C-terminal fragment containing two C2-like domains shows the similar effect, but to a lesser extent, whereas overexpression of full-length Doc2 or the C-terminal fragment of rabphilin3 containing two C2-like domains does not show this effect. Because dynein is a minus-end-directed microtubule-based motor protein, these results suggest that Doc2, especially Doc2, plays a role in dynein-dependent intracellular vesicle transport.

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Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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