A quantitative proteomic analysis of cofilin phosphorylation in myeloid cells and its modulation using the LIM kinase inhibitor Pyr1

• Published in: PloS one Vol. 13; no. 12; p. e0208979
• Main Authors: Prudent, Renaud, Demoncheaux, Nathalie, Diemer, Hélène, Collin-Faure, Véronique, Kapur, Reuben, Paublant, Fabrice, Lafanechère, Laurence, Cianférani, Sarah, Rabilloud, Thierry
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 14.12.2018; Public Library of Science (PLoS)
• Subjects: Actin; Actin Depolymerizing Factors - chemistry; Actin Depolymerizing Factors - metabolism; Actins - metabolism; Amino Acid Sequence; Binding energy; Binding Sites; Biochemistry, Molecular Biology; Biology; Biology and Life Sciences; Breast cancer; Cancer; Cancer treatment; Carbazoles - pharmacology; Cell culture; Cell Line; Cellular signal transduction; Cofilin; Cytoskeleton; Deregulation; Enzyme inhibitors; Genomics; Human evolution; Humans; Inhibition; Kinase inhibitors; Kinases; Leukemia; Life Sciences; LIM kinase; Lim Kinases - antagonists & inhibitors; Metastasis; Microtubules; Muscle proteins; Myeloid cells; Myeloid Cells - drug effects; Myeloid Cells - metabolism; Pharmacology; Phenols (Class of compounds); Phosphorylation; Phosphorylation - drug effects; Physical Sciences; Protein Kinase Inhibitors - pharmacology; Proteins; Proteomics; Regulation; Research and Analysis Methods; Serine; Substrates; Threonine; Tumor cell lines; Tumors; Tyrosine; France

LIM kinases are located at a strategic crossroad, downstream of several signaling pathways and upstream of effectors such as microtubules and the actin cytoskeleton. Cofilin is the only LIM kinases substrate that is well described to date, and its phosphorylation on serine 3 by LIM kinases controls...