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Originally published In Press as doi:10.1074/jbc.M010320200 on January 8, 2001

J. Biol. Chem., Vol. 276, Issue 17, 14059-14066, April 27, 2001
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The 8-kDa Dynein Light Chain Binds to Its Targets via a Conserved (K/R)XTQT Motif*

Kevin W.-H. LoDagger , Scott Naisbitt§, Jing-Song FanDagger , Morgan Sheng§, and Mingjie ZhangDagger ||

From the Dagger  Department of Biochemistry, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, People's Republic of China and the § Howard Hughes Medical Institute and Department of Neurobiology, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts 02114

Cytoplasmic dynein is a large, multisubunit molecular motor that translocates cargoes toward the minus ends of microtubules. Proper functioning of the dynein motor requires precise assembly of its various subunits. Using purified recombinant proteins, we show that the highly conserved 8-kDa light chain (DLC8) binds to the intermediate chain of the dynein complex. The DLC8-binding region was mapped to a highly conserved 10-residue fragment (amino acid sequence SYSKETQTPL) C-terminal to the second alternative splicing site of dynein intermediate chain. Yeast two-hybrid screening using DLC8 as bait identified numerous additional DLC8-binding proteins. Biochemical and mutational analysis of selected DLC8-binding proteins revealed that DLC8 binds to a consensus sequence containing a (K/R)XTQT motif. The (K/R)XTQT motif interacts with the common target-accepting grooves of DLC8 dimer. The role of each conserved amino acid residue in this pentapeptide motif in supporting complex formation with DLC8 was systematically studied using site-directed mutagenesis.

* This work was partially supported by Grants HKUST6084/98M, 6198/99M, and 6207/00M from the Research Grant Council of Hong Kong to M. Z.) and by the Human Frontier Science Program.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Assistant Investigator of the Howard Hughes Medical Institute.

|| To whom correspondence should be addressed. Tel.: 852-2358-8709; Fax: 852-2358-1552; E-mail: mzhang@ust.hk.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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