ArticleThe EMBO journal1996
Activation of Dictyostelium myosin light chain kinase A by phosphorylation of Thr166.
Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 31 citations in OpenAlex.
- Actin-binding domain of Rng2 sparsely bound on F-actin strongly inhibits actin movement on myosin II.Life science alliance · 2023Article
- Functional roles of VASP phosphorylation in the regulation of chemotaxis and osmotic stress response.Cytoskeleton (Hoboken, N.J.) · 2010Article
- Biological, biochemical, and kinetic effects of mutations of the cardiomyopathy loop of Dictyostelium myosin II: importance of ALA400.The Journal of biological chemistry · 2005Article
- Blebbistatin and blebbistatin-inactivated myosin II inhibit myosin II-independent processes in Dictyostelium.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- A novel cGMP signalling pathway mediating myosin phosphorylation and chemotaxis in Dictyostelium.The EMBO journal · 2002Article
- Identification of four candidate cGMP targets in Dictyostelium.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Chimeras of Dictyostelium myosin II head and neck domains with Acanthamoeba or chicken smooth muscle myosin II tail domain have greatly increased and unregulated actin-dependent MgATPase activity.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Cooperativity between two heads of dictyostelium myosin II in in vitro motility and ATP hydrolysis.Biophysical journal · 1999Article
- Filament structure as an essential factor for regulation of Dictyostelium myosin by regulatory light chain phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Nucleotide-dependent conformational change near the fulcrum region in Dictyostelium myosin II.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- MLCK-A, an unconventional myosin light chain kinase from Dictyostelium, is activated by a cGMP-dependent pathway.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Phosphorylation of the regulatory light chain is an important mechanism for the activation of myosin in non-muscle cells. Unlike most myosin light chain kinases (MLCKs), MLCK-A from Dictyostelium is not activated by Ca2+/calmodulin. Autophosphorylation increases activity, but only to a low level, suggesting that there is an additional activation mechanism. Here, we show that MLCK-A is autophosphorylated on Thr289, which is C-terminal to the catalytic domain. Phosphorylation of MLCK-A increases in response to concanavalin A (conA) treatment of cells, which was previously shown to activate MLCK-A. However, a mutant kinase with an alanine at position 289 (T289A) is also phosphorylated in vivo, indicating that there is an additional phosphorylated residue. Based on comparisons with other protein kinases, we tested whether phosphorylation of Thr166 drives activation of MLCK-A. Our data indicate that phosphorylation of Thr289 occurs in vivo, but is not associated with conA-induced activation, whereas phosphorylation of Thr166 by some as yet unidentified kinase is associated with activation. Replacement of Thrl66 with glutamate results in a 12-fold increase in activity as compared with the wild-type enzyme, supporting the idea that phosphorylation of Thr166 increases MLCK-A activity.
Indexed as
Identifiers
8947030PMC452429W106546457What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.