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Originally published as MBC in Press, 10.1091/mbc.E08-05-0483 on September 17, 2008

Vol. 19, Issue 11, 4918-4929, November 2008

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Dynein Light Intermediate Chain: An Essential Subunit That Contributes to Spindle Checkpoint Inactivation

Sarah Mische*, Yungui He*, Lingzhi Ma, Mingang Li, Madeline Serr, and Thomas S. Hays

Department of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, MN 55455

Submitted May 15, 2008; Revised August 22, 2008; Accepted September 5, 2008
Monitoring Editor: Kerry S. Bloom

The dynein light intermediate chain (LIC) is a subunit unique to the cytoplasmic form of dynein, but how it contributes to dynein function is not fully understood. Previous work has established that the LIC homodimer binds directly to the dynein heavy chain and may mediate the attachment of dynein to centrosomes and other cargoes. Here, we report our characterization of the LIC in Drosophila. Unlike vertebrates, in which two Lic genes encode multiple subunit isoforms, the Drosophila LIC is encoded by a single gene. We determined that the single LIC polypeptide is phosphorylated, and that different phosphoisoforms can assemble into the dynein motor complex. Our mutational analyses demonstrate that, similar to other dynein subunits, the Drosophila LIC is required for zygotic development, germline specification of the oocyte, and mitotic cell division. We show that RNA interference depletion of LIC in Drosophila S2 cells does not block the recruitment of a dynein complex to kinetochores, but it does delay inactivation of Mad2 signaling and mitotic progression. Our observations suggest the LIC contributes to a broad range of dynein functions.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E08-05-0483) on September 17, 2008.

* These authors contributed equally to this work.

Address correspondence to: Thomas S. Hays (haysx001{at}umn.edu)

Abbreviations used: LIC, dynein light intermediate chain.




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