ArticleMolecular biology of the cell2006
Caenorhabditis elegans kettin, a large immunoglobulin-like repeat protein, binds to filamentous actin and provides mechanical stability to the contractile apparatuses in body wall muscle.
Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 30 citations in OpenAlex.
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- Mutual dependence between tropomodulin and tropomyosin in the regulation of sarcomeric actin assembly in Caenorhabditis elegans striated muscle.European journal of cell biology · 2022Article
- Kettin, the large actin-binding protein with multiple immunoglobulin domains, is essential for sarcomeric actin assembly and larval development in Caenorhabditis elegans.The FEBS journal · 2020Article
- Tissue-specific transcriptomics and proteomics of a filarial nematode and its Wolbachia endosymbiont.BMC genomics · 2015Article
- Drebrin-like protein DBN-1 is a sarcomere component that stabilizes actin filaments during muscle contraction.Nature communications · 2015Article
- UNC-87 isoforms, Caenorhabditis elegans calponin-related proteins, interact with both actin and myosin and regulate actomyosin contractility.Molecular biology of the cell · 2015Article
- A Proteomic Analysis of the Body Wall, Digestive Tract, and Reproductive Tract of Brugia malayi.PLoS neglected tropical diseases · 2015Article
- Regulation of structure and function of sarcomeric actin filaments in striated muscle of the nematode Caenorhabditis elegans.Anatomical record (Hoboken, N.J. : 2007) · 2014Review
- CPNA-1, a copine domain protein, is located at integrin adhesion sites and is required for myofilament stability in Caenorhabditis elegans.Molecular biology of the cell · 2013Article
- Electron microscopy and 3D reconstruction reveals filamin Ig domain binding to F-actin.Journal of molecular biology · 2012Article
- Removal of Polycomb repressive complex 2 makes C. elegans germ cells susceptible to direct conversion into specific somatic cell types.Cell reports · 2012Article
- Dynamic regulation of sarcomeric actin filaments in striated muscle.Cytoskeleton (Hoboken, N.J.) · 2010Review
- Extensive and modular intrinsically disordered segments in C. elegans TTN-1 and implications in filament binding, elasticity and oblique striation.Journal of molecular biology · 2010Article
- Troponin I controls ovulatory contraction of non-striated actomyosin networks in the C. elegans somatic gonad.Journal of cell science · 2010Article
- A monoclonal antibody toolkit for C. elegans.PloS one · 2010Article
- Cytoplasmic Ig-domain proteins: cytoskeletal regulators with a role in human disease.Cell motility and the cytoskeleton · 2009Review
- Actin-ADF/cofilin rod formation in Caenorhabditis elegans muscle requires a putative F-actin binding site of ADF/cofilin at the C-terminus.Cell motility and the cytoskeleton · 2009Article
- The ALP-Enigma protein ALP-1 functions in actin filament organization to promote muscle structural integrity in Caenorhabditis elegans.Molecular biology of the cell · 2009Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
Kettin is a large actin-binding protein with immunoglobulin-like (Ig) repeats, which is associated with the thin filaments in arthropod muscles. Here, we report identification and functional characterization of kettin in the nematode Caenorhabditis elegans. We found that one of the monoclonal antibodies that were raised against C. elegans muscle proteins specifically reacts with kettin (Ce-kettin). We determined the entire cDNA sequence of Ce-kettin that encodes a protein of 472 kDa with 31 Ig repeats. Arthropod kettins are splice variants of much larger connectin/titin-related proteins. However, the gene for Ce-kettin is independent of other connectin/titin-related genes. Ce-kettin localizes to the thin filaments near the dense bodies in both striated and nonstriated muscles. The C-terminal four Ig repeats and the adjacent non-Ig region synergistically bind to actin filaments in vitro. RNA interference of Ce-kettin caused weak disorganization of the actin filaments in body wall muscle. This phenotype was suppressed by inhibiting muscle contraction by a myosin mutation, but it was enhanced by tetramisole-induced hypercontraction. Furthermore, Ce-kettin was involved in organizing the cytoplasmic portion of the dense bodies in cooperation with alpha-actinin. These results suggest that kettin is an important regulator of myofibrillar organization and provides mechanical stability to the myofibrils during contraction.
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