|
|
|
|
|
|
|
||
Department of Biology, University of Utah, Salt Lake City, Utah 84112
Integrin-dependent cell adhesion to specific
extracellular matrix molecules has been demonstrated
to trigger dramatic changes in gene expression that can
affect cell fate. However, little is understood about the
molecular mechanism by which events at sites of cell-
substratum adhesion are communicated to the cell interior to regulate the transcriptional apparatus. By analogy to classical mechanisms of cell surface receptor
function, it seems likely that some components of the
integrin-activated signal transduction machinery will be
colocalized with cell adhesion molecules. Zyxin is a low
abundance phosphoprotein that accumulates with integrins at sites of cell-substratum attachment. Here we show that zyxin exhibits a functional nuclear export signal that is required to keep zyxin concentrated in the
cytoplasm and is sufficient to direct nuclear proteins to
the cytosol. Furthermore, we demonstrate that native
zyxin shuttles between the nucleus and sites of cell adhesion in fibroblasts and is thus an excellent candidate
for relaying information between these two compartments.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
