ArticleProceedings of the National Academy of Sciences of the United States of America1998
MLCK-A, an unconventional myosin light chain kinase from Dictyostelium, is activated by a cGMP-dependent pathway.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 23 citations in OpenAlex.
- Bleb-driven chemotaxis of Dictyostelium cells.The Journal of cell biology · 2014Article
- A subset of signal transduction pathways is required for hippocampal growth cone collapse induced by ephrin-A5.Developmental neurobiology · 2008Article
- Big roles for small GTPases in the control of directed cell movement.The Biochemical journal · 2007Review
- Alpha-naphthoflavone induces vasorelaxation through the induction of extracellular calcium influx and NO formation in endothelium.Naunyn-Schmiedeberg's archives of pharmacology · 2003Article
- A novel cGMP signalling pathway mediating myosin phosphorylation and chemotaxis in Dictyostelium.The EMBO journal · 2002Article
- Nerve growth factor and semaphorin 3A signaling pathways interact in regulating sensory neuronal growth cone motility.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2002Article
- Identification of four candidate cGMP targets in Dictyostelium.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- A cell number-counting factor regulates the cytoskeleton and cell motility in Dictyostelium.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Guanylate cyclase in Dictyostelium discoideum with the topology of mammalian adenylate cyclase.The Biochemical journal · 2001Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Dictyostelium myosin II is activated by phosphorylation of its regulatory light chain by myosin light chain kinase A (MLCK-A), an unconventional MLCK that is not regulated by Ca2+/calmodulin. MLCK-A is activated by autophosphorylation of threonine-289 outside of the catalytic domain and by phosphorylation of threonine-166 in the activation loop by an unidentified kinase, but the signals controlling these phosphorylations are unknown. Treatment of cells with Con A results in quantitative phosphorylation of the regulatory light chain by MLCK-A, providing an opportunity to study MLCK-A's activation mechanism. MLCK-A does not alter its cellular location upon treatment of cells with Con A, nor does it localize to the myosin-rich caps that form after treatment. However, MLCK-A activity rapidly increases 2- to 13-fold when Dictyostelium cells are exposed to Con A. This activation can occur in the absence of MLCK-A autophosphorylation. cGMP is a promising candidate for an intracellular messenger mediating Con A-triggered MLCK-A activation, as addition of cGMP to fresh Dictyostelium lysates increases MLCK-A activity 3- to 12-fold. The specific activity of MLCK-A in cGMP-treated lysates is 210-fold higher than that of recombinant MLCK-A, which is fully autophosphorylated, but lacks threonine-166 phosphorylation. Purified MLCK-A is not directly activated by cGMP, indicating that additional cellular factors, perhaps a kinase that phosphorylates threonine-166, are involved.
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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.