ArticleJournal of muscle research and cell motility1991
Functional implications of the unusual amino acid sequence of the regulatory light chain of Acanthamoeba castellanii myosin-II.
Article in Journal of muscle research and cell motility, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 3 citations in OpenAlex.
- Regulation of the actin-activated MgATPase activity of Acanthamoeba myosin II by phosphorylation of serine 639 in motor domain loop 2.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Expression of a myosin regulatory light chain phosphorylation site mutant complements the cytokinesis and developmental defects of Dictyostelium RMLC null cells.The Journal of cell biology · 1994Article
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Authors and funding
4 authors at 3 institutions in 1 country.
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Abstract
We have determined by protein chemistry methods the amino acid sequence of light chain 2 from Acanthamoeba castellanii myosin-II (ALC2). This is the first reported sequence for any protozoan myosin light chain. ALC2 consists of 154 amino acid residues, including a single residue of His and two residues each of Pro and Tyr, and lacks Cys and Trp. The N-terminus is blocked, and if an N-terminal acetyl group is assumed. ALC2 has a calculated molecular weight of 17,657. ALC2 is an acidic protein, with a calculated net charge of -7 at pH 7. The sequence of ALC2 is most similar to those of the calmodulins (identity approximately 35%), followed by myosin regulatory light chains. ALC2 appears to lack the potential N-terminal phosphorylation site and single Ca(2+)-binding site in region I which are characteristic of most myosin regulatory light chains. Instead, ALC2, unlike any other myosin light chain characterized to date, may have a functional Ca(2+)-binding site only in region II, suggesting a novel role of ALC2 in the Ca2+ regulation of the activity of Acanthamoeba myosin-II.
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