期刊
JOURNAL OF CELL SCIENCE
卷 135, 期 7, 页码 -出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.258764
关键词
Focal adhesions; Paxillin; Paxillin phosphorylation; FAK; Super-resolution microscopy
类别
资金
- Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) [BA 6471/1-1]
- Erasmus Mundus Europhotonics program
- Deutsche Forschungsgemeinschaft under Die Exzellenzstrategie des Bundes und der Lander (Germany's Excellence Strategy) [EXC 2082/1-390761711]
- Schweizerischer Nationalfonds zur Forderung der Wissenschaftlichen Forschung (Swiss National Science Foundation) [310030_185261, 310030L_170112]
- Swiss National Science Foundation (SNF) [310030_185261, 310030L_170112] Funding Source: Swiss National Science Foundation (SNF)
Integrin-mediated adhesions serve as convergence points for multiple signaling pathways. By using super-resolution microscopy, we discovered spatially defined clusters of pPax and pFAK within focal adhesions, providing new insights into the organization and functions of these adhesion structures.
Integrin-mediated adhesions are convergence points for multiple signaling pathways. Their inner structure and diverse functions can be studied with super-resolution microscopy. Here, we examined the spatial organization within focal adhesions by analyzing several adhesion proteins with structured illumination microscopy (SIM). Paxillin (Pax) serves as a scaffold protein and signaling hub in focal adhesions, and focal adhesion kinase (FAK, also known as PTK2) regulates the dynamics of adhesions. We found that their phosphorylated forms, pPax and pFAK, form spot-like, spatially defined clusters within adhesions in several cell lines and confirmed these findings with additional super-resolution techniques. These clusters showed a more regular separation from each other compared with more randomly distributed signals for FAK or paxillin. Mutational analysis indicated that the active (open) FAK conformation is a prerequisite for the pattern formation of pFAK. Live-cell super-resolution imaging revealed that organization in clusters is preserved over time for FAK constructs; however, distance between clusters is dynamic for FAK, while paxillin is more stable. Combined, these data introduce spatial clusters of pPax and pFAK as substructures in adhesions and highlight the relevance of paxillin-FAK binding for establishing a regular substructure in focal adhesions.
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