Epidermal growth factor induces serine phosphorylation of actin
Open Access
- 9 January 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 357 (3) , 251-254
- https://doi.org/10.1016/0014-5793(94)01359-9
Abstract
Stimulation of cells by epidermal growth factor induces a rapid polymerisation of actin in the cortical skeleton. Activation of the EGF‐receptor leads to autophosphorylation and to phosphorylation of specific intracellular substrates. Here we show that actin is phosphorylated in vitro and in vivo upon EGF stimulation. Two‐dimensional phospho‐amino acid analysis shows that phosphorylation occurs on serine, not on tyrosine residues.Keywords
This publication has 26 references indexed in Scilit:
- Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membraneNature, 1994
- Tyrosine Phosphorylation of Actin in Dictyostelium Associated with Cell-Shape ChangesScience, 1993
- The EGF receptor is an actin-binding protein.The Journal of cell biology, 1992
- The epidermal growth factor receptor is associated with actin filamentsExperimental Cell Research, 1992
- Requirement for Specific Protein Kinase Activities during the Rapid Redistribution of F-actin that Precedes the Outgrowth of Neurites in PC12D Cells.Cell Structure and Function, 1992
- Actin-binding proteins involved in the capping of epidermal growth factor receptors in A431 cellsExperimental Cell Research, 1991
- Epidermal growth factor induces the accumulation of calpactin II on the cell surface during membrane rufflingCell Motility, 1990
- Protein kinase C and cAMP‐dependent protein kinase induce opposite effects on actin polymerizabilityFEBS Letters, 1987
- The protein-tyrosine kinase substrate, p81, is homologous to a chicken microvillar core protein.The Journal of cell biology, 1986
- Evidence for phosphorylation of actin by the insulin receptor‐associated protein kinase from human placentaFEBS Letters, 1983