Literature DB >> 7925974

The sevenmaker gain-of-function mutation in p42 MAP kinase leads to enhanced signalling and reduced sensitivity to dual specificity phosphatase action.

C M Bott1, S G Thorneycroft, C J Marshall.   

Abstract

A mammalian mutant MAP kinase, D319N ERK2, analogous to Drosophila melanogaster sevenmaker (rlsem) gain-of-function mutation was shown to have an increased sensitivity to low levels of signalling in vivo. However, the mutation does not lead to an elevated basal kinase activity and still requires activation by MAP kinase kinase (MAPKK) as does wild type ERK2. This increased responsiveness seen in vivo is not due to an increased ability to phosphorylate substrates but appears to reflect a reduced sensitivity to a MAP kinase phosphatase CL100.

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Year:  1994        PMID: 7925974     DOI: 10.1016/0014-5793(94)00958-9

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  43 in total

Review 1.  ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions.

Authors:  Philippe P Roux; John Blenis
Journal:  Microbiol Mol Biol Rev       Date:  2004-06       Impact factor: 11.056

Review 2.  The ERK cascade: a prototype of MAPK signaling.

Authors:  Hadara Rubinfeld; Rony Seger
Journal:  Mol Biotechnol       Date:  2005-10       Impact factor: 2.695

3.  Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3.

Authors:  Sijiu Liu; Jin-Peng Sun; Bo Zhou; Zhong-Yin Zhang
Journal:  Proc Natl Acad Sci U S A       Date:  2006-03-27       Impact factor: 11.205

4.  Two adjacent docking sites in the yeast Hog1 mitogen-activated protein (MAP) kinase differentially interact with the Pbs2 MAP kinase kinase and the Ptp2 protein tyrosine phosphatase.

Authors:  Yulia Murakami; Kazuo Tatebayashi; Haruo Saito
Journal:  Mol Cell Biol       Date:  2008-01-22       Impact factor: 4.272

5.  Active ERK2 is sufficient to mediate growth arrest and differentiation signaling.

Authors:  Pui-Kei Wu; Seung-Keun Hong; Seung-Hee Yoon; Jong-In Park
Journal:  FEBS J       Date:  2015-02-03       Impact factor: 5.542

6.  DEF pocket in p38α facilitates substrate selectivity and mediates autophosphorylation.

Authors:  Netanel Tzarum; Nadav Komornik; Dorin Ben Chetrit; David Engelberg; Oded Livnah
Journal:  J Biol Chem       Date:  2013-05-13       Impact factor: 5.157

7.  Gonadotropin-releasing hormone and protein kinase C signaling to ERK: spatiotemporal regulation of ERK by docking domains and dual-specificity phosphatases.

Authors:  Stephen Paul Armstrong; Christopher James Caunt; Craig Alexander McArdle
Journal:  Mol Endocrinol       Date:  2009-01-29

8.  A Novel Class of Common Docking Domain Inhibitors That Prevent ERK2 Activation and Substrate Phosphorylation.

Authors:  Rachel M Sammons; Nicole A Perry; Yangmei Li; Eun Jeong Cho; Andrea Piserchio; Diana P Zamora-Olivares; Ranajeet Ghose; Tamer S Kaoud; Ginamarie Debevec; Chandra Bartholomeusz; Vsevolod V Gurevich; Tina M Iverson; Marc Giulianotti; Richard A Houghten; Kevin N Dalby
Journal:  ACS Chem Biol       Date:  2019-05-13       Impact factor: 5.100

9.  Combination of two activating mutations in one HOG1 gene forms hyperactive enzymes that induce growth arrest.

Authors:  Gilad Yaakov; Michal Bell; Stefan Hohmann; David Engelberg
Journal:  Mol Cell Biol       Date:  2003-07       Impact factor: 4.272

10.  Isolation of intrinsically active (MEK-independent) variants of the ERK family of mitogen-activated protein (MAP) kinases.

Authors:  Vered Levin-Salomon; Konstantin Kogan; Natalie G Ahn; Oded Livnah; David Engelberg
Journal:  J Biol Chem       Date:  2008-10-01       Impact factor: 5.157

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