551. 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.
- Author
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Broday L, Kolotuev I, Didier C, Bhoumik A, Podbilewicz B, and Ronai Z
- Subjects
- Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Caenorhabditis elegans Proteins chemistry, Caenorhabditis elegans Proteins genetics, Carrier Proteins chemistry, Carrier Proteins genetics, Cell Adhesion, Intracellular Signaling Peptides and Proteins, Molecular Sequence Data, Muscles physiology, Protein Biosynthesis, RNA, Antisense genetics, RNA, Antisense metabolism, RNA, Small Interfering, Recombinant Fusion Proteins metabolism, Reverse Transcriptase Polymerase Chain Reaction, Transcription, Genetic, Caenorhabditis elegans physiology, Caenorhabditis elegans Proteins metabolism, Carrier Proteins metabolism
- Abstract
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/beta-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.
- Published
- 2004
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