Please use this identifier to cite or link to this item: https://doi.org/10.1242/jcs.172643
Title: Nuclear transport of paxillin depends on focal adhesion dynamics and FAT domains
Authors: Sathe, A.R 
Shivashankar, G.V 
Sheetz, M.P 
Keywords: focal adhesion kinase
focal adhesion kinase 1
focal adhesion targeting protein
paxillin
unclassified drug
vinculin
fibronectin
focal adhesion kinase 1
paxillin
protein binding
PTK2 protein, human
vinculin
Article
fluorescence recovery after photobleaching
focal adhesion
priority journal
protein binding
protein domain
protein function
protein localization
protein transport
cell adhesion
fibroblast
focal adhesion
gene inactivation
genetics
human
metabolism
nucleocytoplasmic transport
Active Transport, Cell Nucleus
Cell Adhesion
Fibroblasts
Fibronectins
Focal Adhesion Kinase 1
Focal Adhesions
Gene Knockout Techniques
Humans
Paxillin
Protein Binding
Protein Domains
Vinculin
Issue Date: 2016
Publisher: Company of Biologists Ltd
Citation: Sathe, A.R, Shivashankar, G.V, Sheetz, M.P (2016). Nuclear transport of paxillin depends on focal adhesion dynamics and FAT domains. Journal of Cell Science 129 (10) : 1981-1988. ScholarBank@NUS Repository. https://doi.org/10.1242/jcs.172643
Rights: Attribution 4.0 International
Abstract: The nuclear transport of paxillin appears to be crucial for paxillin function but the mechanism of transport remains unclear. Here, we show that the nuclear transport of paxillin is regulated by focal adhesion turnover and the presence of FAT domains. Focal adhesion turnover was controlled using triangular or circular fibronectin islands. Circular islands caused higher focal adhesion turnover and increased the nuclear transport of paxillin relative to triangular islands. Mutating several residues of paxillin had no effect on its nuclear transport, suggesting that the process is controlled by multiple domains. Knocking out FAK (also known as PTK2) and vinculin caused an increase in nuclear paxillin. This could be reversed by rescue with wild-type FAK but not by FAK with a mutated FAT domain, which inhibits paxillin binding. Expressing just the FAT domain of FAK not only brought down nuclear levels of paxillin but also caused a large immobile fraction of paxillin to be present at focal adhesions, as demonstrated by fluorescence recovery after photobleaching (FRAP) studies. Taken together, focal adhesion turnover and FAT domains regulate the nuclear localization of paxillin, suggesting a possible role for transcriptional control, through paxillin, by focal adhesions. © 2016.
Source Title: Journal of Cell Science
URI: https://scholarbank.nus.edu.sg/handle/10635/179573
ISSN: 0021-9533
DOI: 10.1242/jcs.172643
Rights: Attribution 4.0 International
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