Publication Type |
Journal Article |
School or College |
College of Science |
Department |
Biology |
Creator |
Beckerle, Mary C. |
Other Author |
Nix, David A. |
Title |
Nuclear-cytoplasmic shuttling of the focal contact protein, zyxin: a potential mechanism for communication between sites of cell adhesion and the nucleus |
Date |
1997 |
Description |
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 |
Type |
Text |
Publisher |
Rockefeller University Press |
Volume |
138 |
Issue |
5 |
First Page |
1139 |
Last Page |
1147 |
Subject |
Zyxin; Cytosol; Nuclear export signal |
Subject LCSH |
Phosphoproteins; Integrins; Cell adhesion; Cellular signal transduction |
Language |
eng |
Bibliographic Citation |
Nix, D. A., & Beckerle, M. C. (1997). Nuclear-cytoplasmic shuttling of the focal contact protein, zyxin: a potential mechanism for communication between sites of cell adhesion and the nucleus. Journal of Cell Biology, 138(5), 1139-47. |
Rights Management |
(c) Nix, D. A., & Beckerle, M. C., 1997. Originally published in J. Cell Biol., 138(5), 1139-47. http://creativecommons.org/licenses/by-nc-sa/3.0/ |
Format Medium |
application/pdf |
Format Extent |
484,120 bytes |
Identifier |
ir-main,6505 |
ARK |
ark:/87278/s6697mrf |
Setname |
ir_uspace |
ID |
703444 |
Reference URL |
https://collections.lib.utah.edu/ark:/87278/s6697mrf |