PMID- 10085298
OWN - NLM
STAT- MEDLINE
DCOM- 19990610
LR  - 20190508
IS  - 0021-9525 (Print)
IS  - 0021-9525 (Linking)
VI  - 144
IP  - 5
DP  - 1999 Mar 8
TI  - Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly,
      migration, and cytokinesis in fibroblasts.
PG  - 1019-31
AB  - In this article, we show that, in transfected COS-1 cells, protein tyrosine
      phosphatase (PTP)-PEST translocates to the membrane periphery following
      stimulation by the extracellular matrix protein fibronectin. When plated on
      fibronectin, PTP-PEST (-/-) fibroblasts display a strong defect in motility. 3 h 
      after plating on fibronectin, the number and size of vinculin containing focal
      adhesions were greatly increased in the homozygous PTP-PEST mutant cells as
      compared with heterozygous cells. This phenomenon appears to be due in part to a 
      constitutive increase in tyrosine phosphorylation of p130(CAS), a known PTP-PEST 
      substrate, paxillin, which associates with PTP-PEST in vitro, and focal adhesion 
      kinase (FAK). Another effect of this constitutive hyperphosphorylation,
      consistent with the focal adhesion regulation defect, is that (-/-) cells spread 
      faster than the control cell line when plated on fibronectin. In the PTP-PEST
      (-/-) cells, an increase in affinity for the SH2 domains of Src and Crk towards
      p130(CAS) was also observed. In (-/-) cells, we found a significant increase in
      the level of tyrosine phosphorylation of PSTPIP, a cleavage furrow-associated
      protein that interacts physically with all PEST family members. An effect of
      PSTPIP hyperphosphorylation appears to be that some cells remain attached at the 
      site of the cleavage furrow for an extended period of time. In conclusion, our
      data suggest PTP-PEST plays a dual role in cell cytoskeleton organization, by
      promoting the turnover of focal adhesions required for cell migration, and by
      directly or indirectly regulating the proline, serine, threonine phosphatase
      interacting protein (PSTPIP) tyrosine phosphorylation level which may be involved
      in regulating cleavage furrow formation or disassembly during normal cell
      division.
FAU - Angers-Loustau, A
AU  - Angers-Loustau A
AD  - Department of Biochemistry, McGill University, Montreal, Quebec, Canada H3G 1Y6.
FAU - Cote, J F
AU  - Cote JF
FAU - Charest, A
AU  - Charest A
FAU - Dowbenko, D
AU  - Dowbenko D
FAU - Spencer, S
AU  - Spencer S
FAU - Lasky, L A
AU  - Lasky LA
FAU - Tremblay, M L
AU  - Tremblay ML
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Cell Biol
JT  - The Journal of cell biology
JID - 0375356
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Cytoskeletal Proteins)
RN  - 0 (Fibronectins)
RN  - 0 (Paxillin)
RN  - 0 (Phosphoproteins)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.10.2 (Focal Adhesion Protein-Tyrosine Kinases)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatase, Non-Receptor Type 12)
RN  - EC 3.1.3.48 (Protein Tyrosine Phosphatases)
SB  - IM
MH  - Animals
MH  - COS Cells
MH  - Cell Adhesion Molecules/*metabolism
MH  - *Cell Cycle
MH  - Cell Membrane/enzymology
MH  - *Cell Movement
MH  - Cytoplasm/enzymology
MH  - Cytoskeletal Proteins/metabolism
MH  - Fibroblasts/cytology/enzymology
MH  - Fibronectins/metabolism
MH  - Focal Adhesion Protein-Tyrosine Kinases
MH  - Paxillin
MH  - Phosphoproteins/metabolism
MH  - Phosphorylation
MH  - Protein Tyrosine Phosphatase, Non-Receptor Type 12
MH  - Protein Tyrosine Phosphatases/*metabolism
MH  - Protein-Tyrosine Kinases/*metabolism
MH  - src Homology Domains
PMC - PMC2148201
EDAT- 1999/03/23 00:00
MHDA- 1999/03/23 00:01
CRDT- 1999/03/23 00:00
PHST- 1999/03/23 00:00 [pubmed]
PHST- 1999/03/23 00:01 [medline]
PHST- 1999/03/23 00:00 [entrez]
AID - 10.1083/jcb.144.5.1019 [doi]
PST - ppublish
SO  - J Cell Biol. 1999 Mar 8;144(5):1019-31. doi: 10.1083/jcb.144.5.1019.