期刊
BIOPHYSICAL JOURNAL
卷 102, 期 9, 页码 2022-2030出版社
CELL PRESS
DOI: 10.1016/j.bpj.2012.01.062
关键词
-
类别
资金
- National Science Foundation [CBET 0955291, DGE 1106400]
- Directorate For Engineering [0955291] Funding Source: National Science Foundation
- Div Of Chem, Bioeng, Env, & Transp Sys [0955291] Funding Source: National Science Foundation
Vinculin phosphorylation has been implicated as a potential mechanism for focal adhesion growth and maturation. Four vinculin residues-Y100, S1033, S1045, and Y1065-are phosphorylated by kinases during focal adhesion maturation. In this study, phosphorylation at each of these residues is simulated using molecular dynamics models. The simulations demonstrate that once each phosphorylated vinculin structure is at equilibrium, significant local conformational changes result that may impact either vinculin activation or vinculin binding to actin and PIP2. Simulation of vinculin activation after phosphorylation shows that the added phosphoryl groups can prime vinculin for activation. It remains to be seen if vinculin can be phosphorylated at S1033 in vivo, but these simulations highlight that in the event of a S1033 phophorylation vinculin will likely be primed for activation.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据