JBC PeproTech; Our Business is Cytokines!

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M006375200 on September 8, 2000

J. Biol. Chem., Vol. 275, Issue 48, 37619-37627, December 1, 2000
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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
Right arrow Citation Map
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?

Low Molecular Weight Protein-tyrosine Phosphatase Controls the Rate and the Strength of NIH-3T3 Cells Adhesion through Its Phosphorylation on Tyrosine 131 or 132*

Paola Chiarugi, Maria Letizia Taddei, Paolo Cirri, Doriana Talini, Francesca Buricchi, Guido Camici, Giampaolo Manao, Giovanni Raugei, and Giampietro RamponiDagger

From the Dipartimento di Scienze Biochimiche, Università degli studi di Firenze, 50134 Firenze, Italy

The low molecular weight protein-tyrosine phosphatase (LMW-PTP) is an enzyme involved in platelet-derived growth factor (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 LMW-PTP activity about 20-fold. 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 regulate 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 signaling. 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, down-regulating matrix metalloproteases 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.

* This work was supported by Consiglio Nazionale delle Ricerche (CNR) Grant 97.03810.CT14 and by a target project on biotechnology, by the Italian Association for Cancer Research and supported in part by the Ministero della Università e Ricerca Scientifica e Tecnologica, CNR strategic project (Controlli Post-trascrizionali dell'Espressione Genica), by European Community Grant ERB-Bo4-CT96-0517, and by Cassa di risparmio di Firenze.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dipartimento di Scienze Biochimiche, viale Morgagni 50, 50134 Firenze, Italy. Tel.: 39-055-413765; Fax: 39-055-4222725; E-mail: ramponi@scibio.unifi.it.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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 TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.