Scaffolding proteins and non-proliferative functions of ERK1/2.
Studies of ERK1/2 generally focus on the regulation of nuclear ERK1/2 function mainly related to proliferation, whereas less attention has been drawn to the role ERK1/2 plays in the cytosol. Scaffolding proteins for ERK1/2 have been shown to control the time point and also the intracellular location of ERK1/2 activation. Hence, by concentrating ERK1/2 within subcellular compartments, scaffolding proteins restrict the substrate specificity of ERK1/2 and thus optimize the cell response for specific signal transduction programs in order to manipulate specific cellular functions. We have presented evidence that the F-actin binding protein calponin represents a new type of ERK1/2 scaffold, controlling the activation of a subfraction of ERK1/2 which is connected solely to contractile and/or migratory events in a cell.
Appel
Sarah
S
Department of Health Sciences; Boston University; Boston, MA USA.
Morgan
Kathleen G
KG
Exp Cell Res. 1999 Nov 25;253(1):255-70
10579927
J Cell Mol Med. 2008 Dec;12(6A):2165-80
19120701
Mol Cell. 2008 Sep 5;31(5):708-21
18775330
Int J Biochem Cell Biol. 2008;40(12):2707-19
18562239
Cell Signal. 1993 Nov;5(6):677-86
8130072
Oncogene. 2007 May 14;26(22):3185-202
17496915
Biochem J. 1999 Nov 15;344 Pt 1:117-23
10548541
Crit Rev Eukaryot Gene Expr. 2008;18(2):93-124
18304026
Oncogene. 2007 May 14;26(22):3122-42
17496911
J Physiol. 2001 Dec 1;537(Pt 2):567-77
11731586
Biochem Soc Trans. 2004 Jun;32(Pt3):438-42
15157155
Cell. 1998 May 15;93(4):605-15
9604935
J Biol Chem. 2009 Jun 26;284(26):17607-15
19406750
J Biol Chem. 2006 Mar 10;281(10):6664-72
16317011
Eur J Cell Biol. 2006 Apr;85(3-4):305-9
16546574