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MBC in Press, published online ahead of print August 29, 2007
Mol. Biol. Cell 10.1091/mbc.E07-03-0278

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Submitted on March 27, 2007
Revised on August 10, 2007
Accepted on August 20, 2007

Two LIM Domain Proteins and UNC-96 Link UNC-97/PINCH to Myosin Thick Filaments in Caenorhabditis elegans Muscle

Hiroshi Qadota,* Kristina B. Mercer,* Rachel K. Miller,* Kozo Kaibuchi,{dagger} and Guy M. Benian*

*Department of Pathology, Emory University, Atlanta, GA 30322; {dagger}Department of Cell Pharmacology, Nagoya University, Graduate School of Medicine, 65 Tsurumai, Showa, Nagoya, Aichi 466-8550, Japan

Monitoring Editor: Erika Holzbaur

By yeast two hybrid screening, we found three novel interactors (UNC-95, LIM-8, and LIM-9) for UNC-97/PINCH in C. elegans. All three proteins contain LIM domains that are required for binding. Among the three interactors, LIM-8 and LIM-9 also bind to UNC-96, a component of sarcomeric M-lines. UNC-96 and LIM-8 also bind to the C-terminal portion of a myosin heavy chain, MHC A, which resides in the middle of thick filaments in the proximity of M-lines. All interactions identified by yeast two hybrid assays were confirmed by in vitro binding assays using purified proteins. All three novel UNC-97 interactors are expressed in body wall muscle and by antibodies localize to M-lines. Either a decreased or an increased dosage of UNC-96 results in disorganization of thick filaments. Our previous studies showed that UNC-98, a C2H2 Zn finger protein, acts as a linkage between UNC-97, an integrin associated protein, and MHC A in myosin thick filaments. In this study, we demonstrate another mechanism by which this linkage occurs: from UNC-97 through LIM-8 or LIM-9/UNC-96 to myosin.

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




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