p60v-src causes tyrosine phosphorylation and inactivation of the N-cadherin-catenin cell adhesion system.

Hamaguchi, Michinari; Matsuyoshi, Norihisa; Ohnishi, Yasuharu; Gotoh, Bin; Takeichi, Masatoshi; Nagai, Yasuo

doi:10.1002/j.1460-2075.1993.tb05658.x

Cited by 391 publications

(298 citation statements)

References 47 publications

Supporting

Mentioning

283

Contrasting

Order By: Relevance

“…In the huiman gastric cancer cell line, HSC-39, mutation in the f-catenin gene that resulted in complete abolishment of E-cadherin-dependent cell-cell adhesion was observed, and transfection of the f-ctenin gene in the cells fully recovered the cell-cell adhesion (Kawanishi et al, 1995). We have previously reported (Matsuyoshi et al, 1992;Hamaguchi et al, 1993a) that cadherin dependent cell-cell adhesion was strongly erturbed upon tyrosine phosphorylation of f-catenin in RSV-transformed cells where cadherins and catenins were expressed and formed complexes as normal cells. Another pTyr-containing protein, pl20, was also identified as a major pTyr-containing protein in RSVtransformed cells whose phosphorylation closely correlated with cell transformation (Reynolds et al, 1989).…”

Section: Discussionmentioning

confidence: 98%

“…These proteins were known as major components of the cell adhesion system and their tyrosine phosphorylation showed good correlation with transforming activity of v-Src kinase (Schaller et al, 1992;Illic et al, 1995;Matsuyoshi et al, 1992;Hamaguchi et al, 1988Hamaguchi et al, , 1993aIllic et al, 1995;Reynolds et al, 1989Reynolds et al, , 1992. Thus, tyrosine phosphorylation of these proteins may perturb cell-cell adhesion and activate tumour cell movement, invasion and metastasis.…”

mentioning

confidence: 99%

“…Assay of protein concentration, SDS-7.5% polyacrylamide gel electrophoresis (PAGE) and immunoblotting with anti-pTyr antibody were described previously (Hamaguchi et al, 1988(Hamaguchi et al, , 1993a.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Tyrosine phosphorylation of 100-130 kDa proteins in lung cancer correlates with poor prognosis

Nishimura

Machida²,

Imaizumi³

et al. 1996

Br J Cancer

View full text Add to dashboard Cite

Summary To search for the signalling pathways in lung cancer relevant to its aggressive behaviour, we studied tyrosine phosphorylated proteins in lung cancer cell lines and surgical specimens. We found that the profiles of protein phosphorylation were closely matched among these cell lines and cancer tissues of different histological origins, and 100 -130 kDa proteins were the major components of phosphorylated proteins. In surgical specimens, approximately half of the cases showed tyrosine phosphorylation of these proteins in a tumourspecific manner, and phosphorylation of these proteins showed good correlation with the survival length of patients after operation. By immunoprecipitation with specific antibodies, we found that pl25FAK, p120 and ,Bcatenin were the major components of tyrosine-phosphorylated proteins in the surgical specimens. These results suggest that tyrosine phosphorylation of these proteins may play a role in tumour relapse and is available as a clinical marker.

show abstract

Section: Discussionmentioning

confidence: 98%

mentioning

confidence: 99%

See 1 more Smart Citation

Tyrosine phosphorylation of 100-130 kDa proteins in lung cancer correlates with poor prognosis

Nishimura

Machida²,

Imaizumi³

et al. 1996

Br J Cancer

View full text Add to dashboard Cite

show abstract

“…This suggests that multiple kinases and phosphatases regulate cadherin function, possibly each playing a role in a specific tissue and at a specific time during development. Overexpression of the nonreceptor tyrosine kinases Src (Matsuyoshi et al, 1992;Hamaguchi et al, 1993;Behrens et al, 1993), and Fer (Rosato et al, 1998) has been demonstrated to increase tyrosine phosphorylation of ␤-catenin (and p120 ctn ). Furthermore, a dominant-negative Src that interferes with function, or a Src-specific tyrosine kinase inhibitor induce cell-cell adhesion (Owens et al, 2000), further suggesting that Src plays an in vivo role in regulating the phosphotyrosine content of ␤-catenin and that suppression of tyrosine phosphorylation of ␤-catenin promotes formation of cadherin-mediated adhesions.…”

Section: Destabilizing Adhesions: Altering the Balance Between Phosphmentioning

confidence: 99%

Turn‐off, drop‐out: Functional state switching of cadherins

Lilien

Balsamo

Arregui

et al. 2002

Developmental Dynamics

149

116

View full text Add to dashboard Cite

The classic cadherins are a group of calcium dependent, homophilic cell-cell adhesion molecules that drive morphogenetic rearrangements and maintain the integrity of cell groups through the formation of adherens junctions. The formation and maintenance of cadherin-mediated adhesions is a multistep process and mechanisms have evolved to regulate each step. This suggests that functional state switching plays an important role in development. Among the many challenges ahead is to determine the developmental role that functional state switching plays in tissue morphogenesis and to define the roles of each of the several regulatory interactions that participate in switching. One correlate of the loss of cadherinmediated adhesion, the "turn-off" of cadherin function, is the exit, or "drop-out" of cells from neural and epithelial layers and their conversion to a motile phenotype. We suggest that epithelial mesenchymal conversions may be initiated by signaling pathways that result in the loss of cadherin function. Tyrosine phosphorylation of ␤-catenin is one such mechanism. Enhanced phosphorylation of tyrosine residues on ␤-catenin is almost invariably associated with loss of the cadherin-actin connection concomitant with loss of adhesive function. There are several tyrosine kinases and phosphatases that have been shown to have the potential to alter the phosphorylation state of ␤-catenin and thus the function of cadherins. Our laboratory has focused on the role of the nonreceptor tyrosine phosphatase PTP1B in regulating the phosphorylation of ␤-catenin on tyrosine residues. Our data suggest that PTP1B is crucial for maintenance of N-cadherin-mediated adhesions in embryonic neural retina cells. By using an L-cell model system constitutively expressing N-cadherin, we have worked out many of the molecular interactions essential for this regulatory interaction. Extracellular cues that bias this critical regulatory interaction toward increased phosphorylation of ␤-catenin may be a critical component of many developmental events.

show abstract

“…By use of mutant src genes, several cellular proteins have been described as transformation-relevant substrates of v-Src kinase. These include; b-catenin (Hamaguchi et al, 1993a); glycoproteins of 95 kDa and 130 kDa (Hamaguchi et al, 1990;Kozuma et al, 1990); connexin-43 (Crow et al, 1992;Kanemitsu et al, 1997); 120-kDa protein (Linder and Burr, 1988). Thus, mutant src genes have been utilized as an e cient tool to characterize substrate proteins.…”

Section: Introductionmentioning

confidence: 99%

v-Src suppresses SHPS-1 expression via the Ras-MAP kinase pathway to promote the oncogenic growth of cells

et al. 2000

View full text Add to dashboard Cite

We investigated the e ect of cell transformation by v-src on the expression and tyrosine phosphorylation of SHPS-1, a putative docking protein for SHP-1 and SHP-2. We found that transformation by v-src virtually inhibited the SHPS-1 expression at mRNA level. While nontransforming Src kinases including c-Src, nonmyristoylated forms of v-Src had no inhibitory e ect on SHPS-1 expression, transforming Src kinases including wild-type v-Src and chimeric mutant of c-Src bearing vSrc SH3 substantially suppressed the SHPS-1 expression. In cells expressing temperature sensitive mutant of v-Src, suppression of the SHPS-1 expression was temperature-dependent. In contrast, tyrosine phosphorylation of SHPS-1 was rather activated in cells expressing c-Src or nonmyristoylated forms of v-Src. SHPS-1 expression in SR3Y1 was restored by treatment with herbimycin A, a potent inhibitor of tyrosine kinase, or by the expression of dominant negative form of Ras. Contrary, active form of Mek1 markedly suppressed SHPS-1 expression. Finally, overexpression of SHPS-1 in SR3Y1 led to the drastic reduction of anchorage independent growth of the cells. Taken together, our results suggest that the suppression of SHPS-1 expression is a pivotal event for cell transformation by v-src, and the Ras-MAP kinase cascade plays a critical role in the suppression.

show abstract

p60v-src causes tyrosine phosphorylation and inactivation of the N-cadherin-catenin cell adhesion system.

Cited by 391 publications

References 47 publications

Tyrosine phosphorylation of 100-130 kDa proteins in lung cancer correlates with poor prognosis

Tyrosine phosphorylation of 100-130 kDa proteins in lung cancer correlates with poor prognosis

Turn‐off, drop‐out: Functional state switching of cadherins

v-Src suppresses SHPS-1 expression via the Ras-MAP kinase pathway to promote the oncogenic growth of cells

Contact Info

Product

Resources

About