Title: Identification of the regulatory phosphorylation sites in pp42/mitogen-activated protein kinase (MAP kinase).
Abstract: Research Article1 April 1991free access Identification of the regulatory phosphorylation sites in pp42/mitogen-activated protein kinase (MAP kinase). D. M. Payne D. M. Payne Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author A. J. Rossomando A. J. Rossomando Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author P. Martino P. Martino Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author A. K. Erickson A. K. Erickson Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author J. H. Her J. H. Her Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author J. Shabanowitz J. Shabanowitz Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author D. F. Hunt D. F. Hunt Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author M. J. Weber M. J. Weber Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author T. W. Sturgill T. W. Sturgill Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author D. M. Payne D. M. Payne Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author A. J. Rossomando A. J. Rossomando Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author P. Martino P. Martino Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author A. K. Erickson A. K. Erickson Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author J. H. Her J. H. Her Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author J. Shabanowitz J. Shabanowitz Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author D. F. Hunt D. F. Hunt Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author M. J. Weber M. J. Weber Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author T. W. Sturgill T. W. Sturgill Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. Search for more papers by this author Author Information D. M. Payne1, A. J. Rossomando1, P. Martino1, A. K. Erickson1, J. H. Her1, J. Shabanowitz1, D. F. Hunt1, M. J. Weber1 and T. W. Sturgill1 1Department of Internal Medicine and Pharmacology, University of Virginia, Charlottesville 22908. The EMBO Journal (1991)10:885-892https://doi.org/10.1002/j.1460-2075.1991.tb08021.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Mitogen-activated protein kinase (MAP kinase) is a 42 kd serine/threonine protein kinase whose enzymatic activity requires phosphorylation of both tyrosyl and threonyl residues. As a step in elucidating the mechanism(s) for activation of this enzyme, we have determined the sites of regulatory phosphorylation. Following proteolytic digestion of 32P-labeled pp42/MAP kinase with trypsin, only a single phosphopeptide was detected by two-dimensional peptide mapping, and this peptide contained both phosphotyrosine and phosphothreonine. The amino acid sequence of the peptide, including the phosphorylation sites, was determined using a combination of Fourier transform mass spectrometry and collision-activated dissociation tandem mass spectrometry with electrospray ionization. The sequence for the pp42/MAP kinase tryptic phosphopeptide is similar (but not identical) to a sequence present in the ERK1- and KSS1-encoded kinases. The two phosphorylation sites are separated by only a single residue. The regulation of activity by dual phosphorylations at closely spaced threonyl and tyrosyl residues has a functional correlate in p34cdc2, and may be characteristic of a family of protein kinases regulating cell cycle transitions. Previous ArticleNext Article Volume 10Issue 41 April 1991In this issue RelatedDetailsLoading ...