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Originally published as MBC in Press, 10.1091/mbc.E05-01-0018 on June 22, 2005

Vol. 16, Issue 9, 4139-4152, September 2005

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Drosophila Mob Family Proteins Interact with the Related Tricornered (Trc) and Warts (Wts) Kinases

Ying He * {dagger}, Kazuo Emoto {ddagger}, Xiaolan Fang *, Nan Ren *, Xiaojing Tian * §, Yuh-Nung Jan {ddagger}, and Paul N. Adler *

* Department of Biology, Center for Morphogenesis and Regenerative Medicine and Cancer Center, University of Virginia, Charlottesville, VA 22903; {ddagger} Howard Hughes Medical Institute, Department of Physiology and Biochemistry, University of California–San Francisco, San Francisco, CA 94143

Submitted January 10, 2005; Revised May 31, 2005; Accepted June 15, 2005
Monitoring Editor: Marianne Bronner-Fraser

The function of Tricornered (Trc), the Drosophila Ndr (Nuclear Dbf2-related) serine/threonine protein kinase, is required for the normal morphogenesis of a variety of polarized outgrowths including epidermal hairs, bristles, arista laterals, and dendrites. In yeast the Trc homolog Cbk1 needs to bind Mob2 to activate the RAM pathway. In this report, we provide genetic and biochemical data that Drosophila Trc also interacts with and is activated by Drosophila Dmob proteins. In addition, Drosophila Mob proteins appear to interact with the related Warts/Lats kinase, which functions as a tumor suppressor in flies and mammals. Interestingly, the overgrowth tumor phenotype that results from mutations in Dmob1 (mats) was only seen in genetic mosaics and not when the entire animal was mutant. We conclude that unlike in yeast, in Drosophila individual Mob proteins interact with multiple kinases and that individual NDR family kinases interact with multiple Mob proteins. We further provide evidence that Mo25, the Drosophila homolog of the RAM pathway hym1 gene does not function along with Trc.


This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E05-01-0018) on June 22, 2005.

{dagger} Present address: Department of Biochemistry, UT Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, TX 75390.

§ Present address: Department of Biology, Washington University, St. Louis, WA 63130

Address correspondence to: Paul N. Adler (pna{at}virginia.edu).




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