Unknown

Dataset Information

0

A role for the juxtamembrane cytoplasm in the molecular dynamics of focal adhesions.


ABSTRACT: Focal adhesions (FAs) are specialized membrane-associated multi-protein complexes that link the cell to the extracellular matrix and play crucial roles in cell-matrix sensing. Considerable information is available on the complex molecular composition of these sites, yet the regulation of FA dynamics is largely unknown. Based on a combination of FRAP studies in live cells, with in silico simulations and mathematical modeling, we show that the FA plaque proteins paxillin and vinculin exist in four dynamic states: an immobile FA-bound fraction, an FA-associated fraction undergoing exchange, a juxtamembrane fraction experiencing attenuated diffusion, and a fast-diffusing cytoplasmic pool. The juxtamembrane region surrounding FAs displays a gradient of FA plaque proteins with respect to both concentration and dynamics. Based on these findings, we propose a new model for the regulation of FA dynamics in which this juxtamembrane domain acts as an intermediary layer, enabling an efficient regulation of FA formation and reorganization.

SUBMITTER: Wolfenson H 

PROVIDER: S-EPMC2627934 | biostudies-literature | 2009

REPOSITORIES: biostudies-literature

altmetric image

Publications

A role for the juxtamembrane cytoplasm in the molecular dynamics of focal adhesions.

Wolfenson Haguy H   Lubelski Ariel A   Regev Tamar T   Klafter Joseph J   Henis Yoav I YI   Geiger Benjamin B  

PloS one 20090128 1


Focal adhesions (FAs) are specialized membrane-associated multi-protein complexes that link the cell to the extracellular matrix and play crucial roles in cell-matrix sensing. Considerable information is available on the complex molecular composition of these sites, yet the regulation of FA dynamics is largely unknown. Based on a combination of FRAP studies in live cells, with in silico simulations and mathematical modeling, we show that the FA plaque proteins paxillin and vinculin exist in four  ...[more]

Similar Datasets

| S-EPMC2665005 | biostudies-literature
| S-EPMC4675889 | biostudies-literature
| S-EPMC6098073 | biostudies-literature
| S-EPMC2898362 | biostudies-literature
| S-EPMC3078811 | biostudies-literature
| S-EPMC5043008 | biostudies-literature
| S-EPMC5954296 | biostudies-literature
| S-EPMC4935953 | biostudies-literature
| S-EPMC4129417 | biostudies-literature
| S-EPMC9117893 | biostudies-literature