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MBC in Press, published online ahead of print March 12, 2008
Mol. Biol. Cell 10.1091/mbc.E08-01-0053

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Submitted on January 22, 2008
Revised on March 3, 2008
Accepted on March 5, 2008

A Novel Protein Phosphatase is a Binding Partner for the Protein Kinase Domains of UNC-89 (Obscurin) in C. elegans

Hiroshi Qadota,* Lee Anne McGaha,*{dagger} Kristina B. Mercer,* Thomas J. Stark,* Tracey M. Ferrara,* and Guy M. Benian*

*Department of Pathology and {dagger}Graduate Division of Biological and Biomedical Sciences, Emory University, Atlanta, GA 30322

Monitoring Editor: Erika Holzbaur

Mutation of the C. elegans gene unc-89 results in disorganization of muscle A-bands. unc-89 encodes a giant polypeptide (900 kDa) containing two protein kinase domains, PK1 and PK2. Yeast two-hybrid screening using a portion of UNC-89 including PK2, yielded SCPL-1, which contains a CTD phosphatase type domain. In addition to the PK2 domain, interaction with SCPL-1 required the putative autoinhibitory sequence, and Ig and Fn3 domains lying N-terminal of the kinase domain. SCPL-1 also interacts with PK1, and similarly requires the kinase domain and upstream Fn3 and Ig domains. Analogous regions from the two other giant kinases of C. elegans, twitchin and TTN-1, failed to interact with SCPL-1. The interaction between SCPL-1 and either Ig-Fn3-PK2 or Fn3-Ig-PK1 was confirmed by biochemical methods. The scpl-1b promoter is expressed in the same set of muscles as unc-89. Antibodies to SCPL-1 localize to the M-line and a portion of the I-band. Bacterially expressed SCPL-1 proteins have phosphatase activity in vitro with properties similar to previously characterized members of the CTD phosphatase family. RNAi knockdown results in a defect in the function of egg laying muscles. These studies suggest a new role for the CTD phosphatase family, that is, in muscle giant kinase signaling.

Address correspondence to: Guy M. Benian (pathgb{at}emory.edu)






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