Mitogen-activated protein kinase kinase 1 (MKK1) is negatively regulated by threonine phosphorylation

Rossomando, A. J., Dent, P., Sturgill, T. W., Marshak, D. R. (March 1994) Mitogen-activated protein kinase kinase 1 (MKK1) is negatively regulated by threonine phosphorylation. Mol Cell Biol, 14 (3). pp. 1594-602. ISSN 0270-7306 (Print)

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URL: http://www.ncbi.nlm.nih.gov/pubmed/8114697
DOI: 10.1128/MCB.14.3.1594

Abstract

Mitogen-activated protein kinase kinase 1 (MKK1), a dual-specificity tyrosine/threonine protein kinase, has been shown to be phosphorylated and activated by the raf oncogene product as part of the mitogen-activated protein kinase cascade. Here we report the phosphorylation and inactivation of MKK1 by phosphorylation on threonine 286 and threonine 292. MKK1 contains a consensus phosphorylation site for p34cdc2, a serine/threonine protein kinase that regulates the cell division cycle, at Thr-286 and a related site at Thr-292. p34cdc2 catalyzes the in vitro phosphorylation of MKK1 on both of these threonine residues and inactivates MKK1 enzymatic activity. Both sites are phosphorylated in vivo as well. The data presented in this report provide evidence that MKK1 is negatively regulated by threonine phosphorylation.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence CDC2 Protein Kinase/ metabolism Hela Cells Humans MAP Kinase Kinase 1 MAP Kinase Kinase 2 Mitogen-Activated Protein Kinase Kinases Molecular Sequence Data Peptide Mapping Peptides/chemistry Phosphothreonine/metabolism Protein-Serine-Threonine Kinases/ metabolism Protein-Tyrosine Kinase/ metabolism Recombinant Proteins Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > phosphorylation
CSHL Authors:
Communities: CSHL labs
Depositing User: Matt Covey
Date: March 1994
Date Deposited: 07 May 2015 18:27
Last Modified: 07 May 2015 18:27
PMCID: PMC358518
Related URLs:
URI: http://repository.cshl.edu/id/eprint/31455

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