Journal
DEVELOPMENTAL CELL
Volume 52, Issue 5, Pages 631-+Publisher
CELL PRESS
DOI: 10.1016/j.devcel.2020.01.007
Keywords
-
Categories
Funding
- Intramural Research Program of the NIH, NIDCR
- China Scholarship Council (CSC)
- National Natural Science Foundation of China (NSFC) [81572818]
- NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH [ZIADE000718, ZIADE000524] Funding Source: NIH RePORTER
Ask authors/readers for more resources
We have discovered that basement membrane and its major components can induce rapid, strikingly robust fibronectin organization. In this new matrix assembly mechanism, alpha 5 beta 1 integrin-based focal adhesions slide actively on the underlying matrix toward the ventral cell center through the dynamic shortening of myosin IIA-associated actin stress fibers to drive rapid fibronectin fibrillogenesis distal to the adhesion. This mechanism contrasts with classical fibronectin assembly based on stable or fixed-position focal adhesions containing alpha V beta 3 integrins plus alpha 5 beta 1 integrin translocation into proximal fibrillar adhesions. On basement membrane components, these sliding focal adhesions contain standard focal adhesion constituents but completely lack classical alpha V beta 3 integrins. Instead, peripheral alpha 3 beta 1 or alpha 2 beta 1 adhesions mediate initial cell attachment but over time are switched to alpha 5 beta 1 integrin-based sliding focal adhesions to assemble fibronectin matrix. This basement-membrane-triggered mechanism produces rapid fibronectin fibrillogenesis, providing a mechanistic explanation for the well-known widespread accumulation of fibronectin at many organ basement membranes.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available