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..., and later as a major cytoplasmic binding partner for members of the cadherin superfamily of cell – cell adhesion molecules (Reynolds et al., 1994; Shibamoto et al., 1995; Staddon et al., 1995). p120 binds to the so-called ‘‘Juxtamembrane domain’’ (JMD) of E-cadherin, where along with other catenins, it is thought to regulate E-cadherin’s adhesive interactions between cells (Aono et al., 1999; Thoreson et al., 2000; Yap et al., 1998). p120 has been implicated in the mechanism of cadherin clustering, possibly through regulation of Rho-GTPases (Anastasiadis et al., 2000; Grosheva et al., 2001; Noren et al., 2000; reviewed in Anastasiadis and Reynolds, 2001). Like b-catenin, its cousin in the cadherin complex, p120 can also translocate to the nucleus, although its role at this location is unknown (Daniel and Reynolds, 1999; van Hengel et al., 1999). These issues have been reviewed in detail recently (Anastasiadis and Reynolds, 2000, 2001). Most proteins physically or functionally related to p120 and/or the E-cadherin complex are oncogenes or tumor suppressors (e.g. Src-family kinases, receptor tyrosine kinases, E-cadherin, b-catenin, Wnt-1, APC, etc.). 584 Although mechanistic studies support such a r...

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...ding proteins also may be required. For example, cadherins bind to and sequester p120-catenin; cytoplasmic p120-catenin inactivates RhoA, and cadherin binding is thought to inhibit this inactivation (=-=Noren et al., 2000-=-; Anastasiadis and Reynolds, 2001; Grosheva et al., 2001; Magie et al., 2002). This mechanism is consistent with the time courses of p120-catenin localization and RhoA activation in our study. Rho GTP...

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...tion in cis with partners in the membrane remains to be determined. Indeed, one can envisage that Trio may interact with the cadherin– catenin complexes, as it has been reported for the Rho-GEF Vav2 (=-=Noren et al., 2000-=-). Moreover, Trio was originally isolated as a binding partner of the LAR transmembrane tyrosine phosphatase (Debant et al., 1996), and we were able to show that LAR sediments with M-cadherin at the t...

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...al., 1998). However, increased cytoplasmic p120 catenin causes reduced stress fiber formation and increased cell motility via modulation of the activity of the Rho GTPases (Anastasiadis et al., 2000; =-=Noren et al., 2000-=-). AF-6 is a downstream target of Ras, which also binds to the tight junction protein ZO-1 (Yamamoto et al., 1997). Because of the close association of actin with the junctional complex of epithelial ...

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... the early phase of adipogenic differentiation. Thesp120 catenin protein exists in equilibrium between two states -seither bound to the membrane-proximal region of E-cadherinsor free in the cytoplasm =-=(44, 45)-=-. The data clearly indicate thatsp120 catenin distribution depends on its tyrosine phosphorylation state, which is regulated by RPTPμ phos-phatasesactivity. In adipocytes, insulin increases the levels...

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...hology and increases cell motility (for review see Anastasiadis and Reynolds, 2001). These effects are apparently mediated by the ability of p120 to suppress RhoA activity (Anastasiadis et al., 2000; =-=Noren et al., 2000-=-) and induce the activities of the related Rho GTPases Rac1 and Cdc42 (Noren et al., 2000; Grosheva et al., 2001). E-cadherin overexpression blocks the effects of p120 on cell morphology, suggesting t...

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...sociation as a RhoGDI (Rho GDPsDissociation Inhibitor) (61);s2) p120 activates Rac1 via Vav2 RhoGEF (Rhos128sGuanidine nucleotide Exchange Factor) and activated Rac1 indirectly inhibits RhoAsactivity =-=(62)-=-;sand 3) p120 binds to p190A RhoGAP (Rho GTPase ActivatingsProtein), and membrane-localized p190A inhibits RhoA locally (105). My resultssindicate that members of the Xenopus p120-catenin subfamily (e...

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...1, Cdc42, RhoA and RhoG, is another candidate for a Rac1 regulator downstream of E-cadherin. p120ctn, which binds to the membrane-proximal region of the cadherin, interacts with Vav2 in HEK293 cells (=-=Noren et al., 2000-=-). Overexpression of p120ctn activates Rac1 and Cdc42 through Vav2 in CHO cells. Further studies are necessary to elucidate whether, and if so how, Tiam1 or Vav2 are involved in the activation of Rac1...

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...tin stress fibers, lamellipodia and filopodia (Nobes and Hall, 1995). The interaction of p120ctn with Rho family GTPases has been recently described (Anastasiadis et al., 2000; Grosheva et al., 2001; =-=Noren et al., 2000-=-). Transfection experiments have shown that p120ctn can induce a dramatic effect on the morphology of fibroblasts (Reynolds et al., 1996). Specifically, ectopic overexpression of p120ctn was associate...

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...ctin organization when overexpressed in fibroblasts, resulting in generation of multiple filopodia at the cell periphery and stress fiber disruption (Reynolds et al., 1996; Anastasiadis et al., 2000; =-=Noren et al., 2000-=-). However, the reorganization of actin observed upon PKP2 KD was not mimicked by p120 KD (Figure 5, A and B), as p120ctn KD cells exhibited a more condensed cortical actin ring (Figure 5B). Likewise,...