JBC Anatrace, Inc.

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 QUICK SEARCH:   [advanced]


     


A more recent version of this article appeared on November 22, 2000
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
275/48/37619    most recent
M006375200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chiarugi, P.
Right arrow Articles by Ramponi, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chiarugi, P.
Right arrow Articles by Ramponi, G.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print September 8, 2000
J. Biol. Chem, 10.1074/jbc.M006375200
Submitted on July 18, 2000
Accepted on September 8, 2000

LMW-PTP controls the rate and the strenght of NIH-3T3 cells adhesion through its phosphorylation on tyrosine 131 or 132

Paola Chiarugi, Maria L. Taddei, Paolo Cirri, Doriana Talini, Francesca Buricchi, Guido Camici, Giampaolo Manao, Giovanni Raugei, and Giampietro Ramponi

Dipartimento di Scienze Biochimiche, Universita di Firenze, Firenze 50134

Corresponding Author: ramponi{at}scibio.unifi.it

The low molecular weight protein tyrosine phosphatase (LMW-PTP) is an enzyme involved in PDGF-induced mitogenesis and cytoskeleton rearrangement. Our previous results demonstrated that LMW-PTP is able to bind and dephosphorylate activated PDGF receptor, thus inhibiting cell proliferation. Recently we have shown that LMW-PTP is specifically phosphorylated by c-Src in a cytoskeleton-associated fraction in response to PDGF, and this phosphorylation increases about 20-fold LMW-PTP activity. LMW-PTP strongly influences cell adhesion, spreading and chemotaxis induced by PDGF stimulation, by regulating the phosphorylation level of p190Rho-GAP, a protein that is able to regulates Rho activity and hence cytoskeleton rearrangement. In the present study we investigate the physiological role of the two LMW-PTP tyrosine phosphorylation sites, using LMW-PTP mutants on tyrosine 131 or 132. We demonstrate that each tyrosine residue is involved in specific LMW-PTP functions. Both of them are phosphorylated during PDGF signalling. Phosphorylation on tyrosine 131 influences mitogenesis, dephosphorylating activated PDGF-R and cytoskeleton rearrangement, acting on p190RhoGAP. Phosphorylation on tyrosine 132 leads to an increase in the strength of cell substrate adhesion, downregulating matrix metallo-proteases expression, through the inhibition of Grb2/MAPK pathway. In conclusion, LMW-PTP tyrosine phosphorylation on both Tyr131 or Tyr132 cooperate to determine a faster and stronger adhesion to extracellular matrix, although these two events may diverge in timing and relative amount.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
BloodHome page
F. Mancini, S. Rigacci, A. Berti, C. Balduini, and M. Torti
The low-molecular-weight phosphotyrosine phosphatase is a negative regulator of Fc{gamma}RIIA-mediated cell activation
Blood, September 15, 2007; 110(6): 1871 - 1878.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Biol.Home page
K. Kuribayashi, K. Nakamura, M. Tanaka, T. Sato, J. Kato, K. Sasaki, R. Takimoto, K. Kogawa, T. Terui, T. Takayama, et al.
Essential role of protein kinase C {zeta} in transducing a motility signal induced by superoxide and a chemotactic peptide, fMLP
J. Cell Biol., March 26, 2007; 176(7): 1049 - 1060.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
E. Lescop, Y. Hu, H. Xu, W. Hu, J. Chen, B. Xia, and C. Jin
The Solution Structure of Escherichia coli Wzb Reveals a Novel Substrate Recognition Mechanism of Prokaryotic Low Molecular Weight Protein-tyrosine Phosphatases
J. Biol. Chem., July 14, 2006; 281(28): 19570 - 19577.
[Abstract] [Full Text] [PDF]


Home page
J. Bacteriol.Home page
H. Xu, B. Xia, and C. Jin
Solution Structure of a Low-Molecular-Weight Protein Tyrosine Phosphatase from Bacillus subtilis
J. Bacteriol., February 15, 2006; 188(4): 1509 - 1517.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
E. Finkelstein, W. Chang, P.-H. G. Chao, D. Gruber, A. Minden, C. T. Hung, and J. C. Bulinski
Roles of microtubules, cell polarity and adhesion in electric-field-mediated motility of 3T3 fibroblasts
J. Cell Sci., March 15, 2004; 117(8): 1533 - 1545.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Rigacci, E. Rovida, P. D. Sbarba, and A. Berti
Low Mr Phosphotyrosine Protein Phosphatase Associates and Dephosphorylates p125 Focal Adhesion Kinase, Interfering with Cell Motility and Spreading
J. Biol. Chem., October 25, 2002; 277(44): 41631 - 41636.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.