| Interacting proteins: Q93052 and P50552 |
Pubmed |
SVM Score :0.0 |
| Overlay studies demonstrate that LASP 1 directly binds to the proline rich domains of zyxin , lipoma preferred partner ( LPP ) , and vasodilator stimulated phosphoprotein ( VASP ) , with zyxin being the most prominent interacting partner . ^^^ |
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| Interacting proteins: Q93052 and P50552 |
Pubmed |
SVM Score :0.0 |
| LPP localizes in focal adhesions as well as in cell to cell contacts , and it binds VASP , a protein implicated in the control of actin organization . ^^^ |
|
| Interacting proteins: Q93052 and P50552 |
Pubmed |
SVM Score :0.0 |
| We found that the LIM domains are the main focal adhesion targeting elements and that the proline rich region of LPP , which harbors binding sites for alpha actinin and vasodilator stimulated phosphoprotein ( VASP ) , has a weak targeting capacity . ^^^ The proline rich region of LPP contains targeting sites for focal adhesions and stress fibers that are distinct from the alpha actinin and VASP binding sites , and the LPP LIM domains are dispensable for targeting LPP to the nucleus . ^^^ |
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| Interacting proteins: Q93052 and P50552 |
Pubmed |
SVM Score :0.0 |
| Using a quantitative assay for cell cell adhesion , we demonstrate that zyxin and LPP function to increase the rate of early cell cell junction assembly through the VASP binding ActA repeat region . ^^^ Dominant negative zyxin / LPP mutants reduce the rate of adhesion , lower VASP levels in detergent insoluble cadherin actin networks , and allow for the accumulation of capping protein at cell cell contacts . ^^^ These data implicate the LIM domains of zyxin and LPP in regulating cell cell junction assembly through VASP . . ^^^ |
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| Interacting proteins: Q93052 and P50552 |
Pubmed |
SVM Score :0.0 |
| NA |
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