Ordered phosphorylation of p42mapk by MAP kinase kinase.

Published

Journal Article

Preparation of milligram amounts of [32P]p42mapk, phosphorylated at Tyr185 or diphosphorylated at Tyr185/Thr183, for use as specific protein phosphatase substrates is described. Tyr- but not Thr-phosphorylated p42mapk, accumulates when ATP is limiting. Furthermore, Tyr185-phosphorylated p42mapk exhibits an apparent 10-fold decrease in apparent Km (46.6 +/- 6.6 nM) for MAP kinase kinase compared to that for the dephospho form (approximately 476 nM). We conclude that Tyr185 precedes Thr183 phosphorylation, and that this is prerequisite, dramatically increasing the affinity of p42mapk for MAP kinase kinase.

Full Text

Duke Authors

Cited Authors

  • Haystead, TA; Dent, P; Wu, J; Haystead, CM; Sturgill, TW

Published Date

  • July 13, 1992

Published In

Volume / Issue

  • 306 / 1

Start / End Page

  • 17 - 22

PubMed ID

  • 1628739

Pubmed Central ID

  • 1628739

International Standard Serial Number (ISSN)

  • 0014-5793

Digital Object Identifier (DOI)

  • 10.1016/0014-5793(92)80828-5

Language

  • eng

Conference Location

  • England