Journal
JOURNAL OF CELL SCIENCE
Volume 130, Issue 20, Pages 3517-3531Publisher
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.200691
Keywords
Vinexin; CAP; ArgBP2; Focal adhesion; Actin cytoskeleton; Mechanotransduction
Categories
Funding
- Naito Foundation
- Asahi Glass Foundation
- Japan Society for the Promotion of Science [20380186, 24380185, 24658094, 26660291, 16K15090, 12J03633, 09J02878]
- Ministry of Education, Culture, Sports, Science and Technology of Japan [26112707, 25221203]
- Advanced Research and Development Programs for Medical Innovation from the Japan Agency for Medical Research and Development
- US National Institutes of Health [DK60597, 60591]
- Grants-in-Aid for Scientific Research [15H03004, 09J02878, 26660291, 16K12872, 26112707, 20380186, 24658094, 16K15090] Funding Source: KAKEN
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Vinexin, c-Cbl associated protein (CAP) and Arg-binding protein 2 (ArgBP2) constitute an adaptor protein family called the vinexin (SORBS) family that is targeted to focal adhesions (FAs). Although numerous studies have focused on each of the SORBS proteins and partially elucidated their involvement in mechanotransduction, a comparative analysis of their function has not been well addressed. Here, we established mouse embryonic fibroblasts that individually expressed SORBS proteins and analysed their functions in an identical cell context. Both vinexin-a and CAP co-localized with vinculin at FAs and promoted the appearance of vinculin-rich FAs, whereas ArgBP2 co-localized with a-actinin at the proximal end of FAs and punctate structures on actin stress fibers (SFs), and induced paxillin-rich FAs. Furthermore, both vinexin-a and CAP contributed to extracellular matrix stiffness-dependent vinculin behaviors, while ArgBP2 stabilized a-actinin on SFs and enhanced intracellular contractile forces. These results demonstrate the differential roles of SORBS proteins in mechanotransduction.
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