期刊
JOURNAL OF CELL SCIENCE
卷 127, 期 8, 页码 1779-1791出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.139014
关键词
Adhesion; alpha-Catenin; Cadherin; Mechanotransduction
类别
资金
- National Institutes of Health [5RO1 GM0974, 1RO1 GM076561]
- National Science Foundation [CMMI 10-29871]
- Beckman Institute Graduate Fellowship
- American Heart Association Predoctoral Fellowship [10PRE3840004]
- NSF Integrative Graduate Education and Research Traineeship [IGERT 0965918]
- Div Of Civil, Mechanical, & Manufact Inn
- Directorate For Engineering [1029871] Funding Source: National Science Foundation
The findings presented here demonstrate the role of alpha-catenin in cadherin-based adhesion and mechanotransduction in different mechanical contexts. Bead-twisting measurements in conjunction with imaging, and the use of different cell lines and alpha-catenin mutants reveal that the acute local mechanical manipulation of cadherin bonds triggers vinculin and actin recruitment to cadherin adhesions in an actin-and alpha-catenin-dependent manner. The modest effect of alpha-catenin on the two-dimensional binding affinities of cell surface cadherins further suggests that forceactivated adhesion strengthening is due to enhanced cadherincytoskeletal interactions rather than to alpha-catenin-dependent affinity modulation. Complementary investigations of cadherin-based rigidity sensing also suggest that, although alpha-catenin alters traction force generation, it is not the sole regulator of cell contractility on compliant cadherin-coated substrata.
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