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Published 21 June 2004. doi:10.1083/jcb.200401133
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 165, Number 6, 857-867
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Article

The LIM domain protein UNC-95 is required for the assembly of muscle attachment structures and is regulated by the RING finger protein RNF-5 in C. elegans



Limor Broday1,2, Irina Kolotuev2, Christine Didier1, Anindita Bhoumik1, Benjamin Podbilewicz2, and Ze'ev Ronai1

1 Ruttenberg Cancer Center, Mount Sinai School of Medicine, New York, NY 10029
2 Department of Biology, Technion-Israel Institute of Technology, Haifa 32000, Israel

Address correspondence to Ze'ev Ronai, Ruttenberg Cancer Center, Mount Sinai School of Medicine, Box 1130, New York, NY 10029. Tel.: (212) 659-5571. Fax: (212) 849-2425. email: zeev.ronai{at}mssm.edu; or Limor Broday, email: limor.broday{at}mssm.edu

Here, we describe a new muscle LIM domain protein, UNC-95, and identify it as a novel target for the RING finger protein RNF-5 in the Caenorhabditis elegans body wall muscle. unc-95(su33) animals have disorganized muscle actin and myosin-containing filaments as a result of a failure to assemble normal muscle adhesion structures. UNC-95 is active downstream of PAT-3/ß-integrin in the assembly pathways of the muscle dense body and M-line attachments, and upstream of DEB-1/vinculin in the dense body assembly pathway. The translational UNC-95::GFP fusion construct is expressed in dense bodies, M-lines, and muscle–muscle cell boundaries as well as in muscle cell bodies. UNC-95 is partially colocalized with RNF-5 in muscle dense bodies and its expression and localization are regulated by RNF-5. rnf-5(RNAi) or a RING domain deleted mutant, rnf-5(tm794), exhibit structural defects of the muscle attachment sites. Together, our data demonstrate that UNC-95 constitutes an essential component of muscle adhesion sites that is regulated by RNF-5.

Key Words: UNC-95; RNF-5; LIM; RING; E3 ligase

The online version of this article includes supplemental material.

Abbreviations used in this paper: dsRNA, double-stranded RNA; Pat, paralyzed arrest at embryonic two-fold stage; RNAi, RNA interference.


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