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The explorations of dynamic interactions of paxillin at the focal adhesions.

Authors :
Aziz AUR
Deng S
Jin Y
Li N
Zhang Z
Yu X
Liu B
Source :
Biochimica et biophysica acta. Proteins and proteomics [Biochim Biophys Acta Proteins Proteom] 2022 Oct 01; Vol. 1870 (10), pp. 140825. Date of Electronic Publication: 2022 Aug 01.
Publication Year :
2022

Abstract

Paxillin is one of the most important adapters in integrin-mediated adhesions that performs numerous crucial functions relying on its dynamic interactions. Its structural behavior serves different purposes, providing a base for several activities. The various domains of paxillin display different functions in the whole process of cell movements and have a significant role in cell adhesion, migration, signal transmission, and protein-protein interactions. On the other hand, some paxillin-associated proteins provide a unique spatiotemporal mechanism for regulating its dynamic characteristics in the tissue homeostasis and make it a more complex and decisive protein at the focal adhesions. This review briefly describes the structural adaptations and molecular mechanisms of recruitment of paxillin into adhesions, explains paxillin's binding dynamics and impact on adhesion stability and turnover, and reveals a variety of paxillin-associated regulatory mechanisms and how paxillin is embedded into the signaling networks.<br /> (Copyright © 2022 Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
1878-1454
Volume :
1870
Issue :
10
Database :
MEDLINE
Journal :
Biochimica et biophysica acta. Proteins and proteomics
Publication Type :
Academic Journal
Accession number :
35926716
Full Text :
https://doi.org/10.1016/j.bbapap.2022.140825