A Role for Gα12/ Gα13in p120ctnRegulation
The catenin p120 ( p120ctn) is an armadillo repeat domain protein that binds to cadherins and has been shown to facilitate strong cell-cell adhesion. We have investigated a possible link between heterotrimeric G proteins and p120ctn, and found that both Gα12and Gα13can completely and selectively abr...
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Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 101; no. 28; pp. 10314 - 10319 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
National Academy of Sciences
13.07.2004
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Subjects | |
Online Access | Get full text |
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Summary: | The catenin p120 ( p120ctn) is an armadillo repeat domain protein that binds to cadherins and has been shown to facilitate strong cell-cell adhesion. We have investigated a possible link between heterotrimeric G proteins and p120ctn, and found that both Gα12and Gα13can completely and selectively abrogate the p120ctn-induced branching phenotype in different cell types. Consistent with these observations, the expression of Gα12or Gα13compensates for the reduction of Rho activity induced by p120ctn. On the other hand, p120ctncan be selectively coimmunoprecipitated with Gα12, and the coimmunoprecipitation was favored by activation of the G protein. A specific interaction between p120ctnand Gα12Q231 L was also observed in in vitro binding experiments. In addition, p120ctncan be immunoprecipitated along with Gα12Q231 L in L cells in absence of E-cadherin. Interestingly, the expression of Gα12Q231 L increases the amount of p120ctnassociated with E-cadherin. These findings demonstrate that Gα12and p120ctnare binding partners, and they also suggest a role for Gα12in regulating p120ctnactivity and its interaction with cadherins. We propose that the Gα12- p120ctninteraction acts as a molecular switch, which regulates cadherin-mediated cell-cell adhesion. |
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ISSN: | 0027-8424 1091-6490 |