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• W2103294240 endingPage "1971" @default.
• W2103294240 startingPage "1955" @default.
• W2103294240 abstract "Microinjection of the catalytic subunit of cAMP-dependent protein kinase (A-kinase) into living fibroblasts or the treatment of these cells with agents that elevate the intracellular cAMP level caused marked alterations in cell morphology including a rounded phenotype and a complete loss of actin microfilament bundles. These effects were transient and fully reversible. Two-dimensional gel electrophoresis was used to analyze the changes in phosphoproteins from cells injected with A-kinase. These experiments showed that accompanying the disassembly of actin microfilaments, phosphorylation of myosin light chain kinase (MLCK) increased and concomitantly, the phosphorylation of myosin P-light chain decreased. Moreover, inhibiting MLCK activity via microinjection of affinity-purified antibodies specific to native MLCK caused a complete loss of microfilament bundle integrity and a decrease in myosin P-light chain phosphorylation, similar to that seen after injection of A-kinase. These data support the idea that A-kinase may regulate microfilament integrity through the phosphorylation and inhibition of MLCK activity in nonmuscle cells." @default.
• W2103294240 created "2016-06-24" @default.
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• W2103294240 date "1988-06-01" @default.
• W2103294240 modified "2023-10-16" @default.
• W2103294240 title "Regulation of actin microfilament integrity in living nonmuscle cells by the cAMP-dependent protein kinase and the myosin light chain kinase." @default.
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• W2103294240 doi "https://doi.org/10.1083/jcb.106.6.1955" @default.
• W2103294240 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2115126" @default.
• W2103294240 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/3290222" @default.
• W2103294240 hasPublicationYear "1988" @default.
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