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dc.contributor.authorIkebe, Reiko
dc.contributor.authorReardon, Sheila
dc.contributor.authorMitsui, Toshiaki
dc.contributor.authorIkebe, Mitsuo
dc.date2022-08-11T08:10:04.000
dc.date.accessioned2022-08-23T16:54:03Z
dc.date.available2022-08-23T16:54:03Z
dc.date.issued1999-10-09
dc.date.submitted2008-08-04
dc.identifier.citation<p>J Biol Chem. 1999 Oct 15;274(42):30122-6.</p>
dc.identifier.issn0021-9258 (Print)
dc.identifier.doi10.1074/jbc.274.42.30122
dc.identifier.pmid10514500
dc.identifier.urihttp://hdl.handle.net/20.500.14038/42411
dc.description.abstractMyosin regulatory light chain (RLC) is phosphorylated at various sites at its N-terminal region, and heterotrimeric myosin light chain phosphatase (MLCP) has been assigned as a physiological phosphatase that dephosphorylates myosin in vivo. Specificity of MLCP toward the various phosphorylation sites of RLC was studied, as well as the role of the N-terminal region of RLC in the dephosphorylation of myosin by MLCP. MLCP dephosphorylated phosphoserine 19, phosphothreonine 18, and phosphothreonine 9 efficiently with almost identical rates, whereas it failed to dephosphorylate phosphorylated serine 1/serine 2. Deletion of the N-terminal seven amino acid residues of RLC markedly decreased the dephosphorylation rate of phosphoserine 19 of RLC incorporated in the myosin molecule, whereas this deletion did not significantly affect the dephosphorylation rate of isolated RLC. On the other hand, deletion of only four N-terminal amino acid residues showed no effect on dephosphorylation of phosphoserine 19 of incorporated RLC. The inhibition of dephosphorylation by deletion of the seven N-terminal residues was also found with the catalytic subunit of MLCP. Phosphorylation at serine 1/serine 2 and threonine 9 did not influence the dephosphorylation rate of serine 19 and threonine 18 by MLCP. These results suggest that the N-terminal region of RLC plays an important role in substrate recognition of MLCP.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=10514500&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1074/jbc.274.42.30122
dc.subjectAmino Acid Sequence
dc.subjectAnimals
dc.subjectMolecular Sequence Data
dc.subjectMyosin Light Chains
dc.subjectMyosin-Light-Chain Phosphatase
dc.subjectPhosphoprotein Phosphatases
dc.subjectPhosphorylation
dc.subjectProtein Kinase C
dc.subjectSubstrate Specificity
dc.subjectTurkeys
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleRole of the N-terminal region of the regulatory light chain in the dephosphorylation of myosin by myosin light chain phosphatase
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume274
dc.source.issue42
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/763
dc.identifier.contextkey564678
html.description.abstract<p>Myosin regulatory light chain (RLC) is phosphorylated at various sites at its N-terminal region, and heterotrimeric myosin light chain phosphatase (MLCP) has been assigned as a physiological phosphatase that dephosphorylates myosin in vivo. Specificity of MLCP toward the various phosphorylation sites of RLC was studied, as well as the role of the N-terminal region of RLC in the dephosphorylation of myosin by MLCP. MLCP dephosphorylated phosphoserine 19, phosphothreonine 18, and phosphothreonine 9 efficiently with almost identical rates, whereas it failed to dephosphorylate phosphorylated serine 1/serine 2. Deletion of the N-terminal seven amino acid residues of RLC markedly decreased the dephosphorylation rate of phosphoserine 19 of RLC incorporated in the myosin molecule, whereas this deletion did not significantly affect the dephosphorylation rate of isolated RLC. On the other hand, deletion of only four N-terminal amino acid residues showed no effect on dephosphorylation of phosphoserine 19 of incorporated RLC. The inhibition of dephosphorylation by deletion of the seven N-terminal residues was also found with the catalytic subunit of MLCP. Phosphorylation at serine 1/serine 2 and threonine 9 did not influence the dephosphorylation rate of serine 19 and threonine 18 by MLCP. These results suggest that the N-terminal region of RLC plays an important role in substrate recognition of MLCP.</p>
dc.identifier.submissionpathoapubs/763
dc.contributor.departmentDepartment of Physiology
dc.source.pages30122-6


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