TY - JOUR
AU - 
AB - THE JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 275, No. 15, Issue of April 14, pp. 11333–11340, 2000 © 2000 by The American Society for Biochemistry and Molecular Biology, Inc. Printed in U.S.A. Phosphorylation of Paxillin via the ERK Mitogen-activated Protein Kinase Cascade in EL4 Thymoma Cells* (Received for publication, December 31, 1999) Hsun Ku and Kathryn E. Meier‡ From the Department of Cell and Molecular Pharmacology, Medical University of South Carolina, Charleston, South Carolina 29425-2251 Intracellular signals can regulate cell adhesion via Intracellular signaling events also regulate adhesion, in a several mechanisms in a process referred to as “inside- process referred to as “inside-out” signaling (5). For example, out” signaling. In phorbol ester-sensitive EL4 thymoma receptor-mediated signals can “prime” integrins by increasing cells, phorbol-12-myristate 13-acetate (PMA) induces ac- their affinity for ligand (6). Activation of protein kinase C tivation of extracellular signal-regulated kinase (ERK) (PKC) can enhance adhesion via a mechanism that does not mitogen-activated protein kinases and promotes cell ad- require direct phosphorylation of integrin subunits (7). Thus, hesion. In this study, clonal EL4 cell lines with varying phosphorylation events involving multiple components of the abilities to activate ERKs in response to PMA were used focal adhesion complex may 
TI - Phosphorylation of Paxillin via the ERK Mitogen-activated Protein Kinase Cascade in EL4 Thymoma Cells
JF - Journal of Biological Chemistry
DO - 10.1074/jbc.275.15.11333
DA - 2000-04-01
UR - https://www.deepdyve.com/lp/unpaywall/phosphorylation-of-paxillin-via-the-erk-mitogen-activated-protein-SGI6Z00qDM
DP - DeepDyve
ER -