ArticleThe FEBS journal2020
Kettin, the large actin-binding protein with multiple immunoglobulin domains, is essential for sarcomeric actin assembly and larval development in Caenorhabditis elegans.
Article in The FEBS journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 7 citations in OpenAlex.
- Linear Z-line-like alignment of capping protein in obliquely striated muscle of the nematodeMolecular biology of the cell · 2026Article
- Linear Z-line-like alignment of capping protein in obliquely striated muscle of the nematodebioRxiv : the preprint server for biology · 2025Article
- Overexpression of Lifeact in theFrontiers in cell and developmental biology · 2024Article
- The α-arrestin SUP-13/ARRD-15 promotes isoform turnover of actin-interacting protein 1 inPNAS nexus · 2023Article
- Mutual dependence between tropomodulin and tropomyosin in the regulation of sarcomeric actin assembly in Caenorhabditis elegans striated muscle.European journal of cell biology · 2022Article
- The intestinal milieu influences the immunoproteome of male and femaleParasitology · 2020Article
- Segregated localization of two calponin-related proteins within sarcomeric thin filaments in Caenorhabditis elegans striated muscle.Cytoskeleton (Hoboken, N.J.)Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
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Abstract
Among many essential genes in the nematode Caenorhabditis elegans, let-330 is located on the left arm of chromosome V and was identified as the largest target of a mutagen in this region. However, let-330 gene has not been characterized at the molecular level. Here, we report that two sequenced let-330 alleles are nonsense mutations of ketn-1, a previously characterized gene encoding kettin. Kettin is a large actin-binding protein of 472 kDa with 31 immunoglobulin domains and is expressed in muscle cells in C. elegans. let-330/ketn-1 mutants are homozygous lethal at the first larval stage with mild defects in body elongation. These mutants have severe defects in sarcomeric actin and myosin assembly in striated muscle. However, α-actinin and vinculin, which are components of the dense bodies anchoring actin to the membranes, were not significantly disorganized by let-330/ketn-1 mutation. Kettin localizes to embryonic myofibrils before α-actinin is expressed, and α-actinin deficiency does not affect kettin localization in larval muscle. Depletion of vinculin minimally affects kettin localization but significantly reduces colocalization of actin with kettin in embryonic muscle cells. These results indicate that kettin is an essential protein for sarcomeric assembly of actin filaments in muscle cells.
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