Reference - Detail
|Author||Broday L, Kolotuev I, Didier C, Bhoumik A, Podbilewicz B, Ronai Z.|
|Title||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.|
|Journal||J. Cell Biol.|
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.
|MeSH||Amino Acid Sequence Animals Base Sequence Binding Sites Caenorhabditis elegans / physiology* Caenorhabditis elegans Proteins / chemistry Caenorhabditis elegans Proteins / genetics Caenorhabditis elegans Proteins / metabolism* Carrier Proteins / chemistry Carrier Proteins / genetics Carrier Proteins / metabolism* 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|
|WOS Category||CELL BIOLOGY|