Open AccessVinexin family (SORBS) proteins play different roles in stiffness-sensing and contractile force generation
Author(s) -
Takafumi Ichikawa,
Masahiro Kita,
Tsubasa S. Matsui,
Ayaka Ichikawa Nagasato,
Tomohiko Araki,
Shian-Huey Chiang,
Takuhito Sezaki,
Yasuhisa Kimura,
Kazumitsu Ueda,
Shinji Deguchi,
Alan R. Saltiel,
Noriyuki Kioka
Publication year - 2017
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.200691
Subject(s) - vinculin , signal transducing adaptor protein , microbiology and biotechnology , focal adhesion , mechanotransduction , paxillin , biology , extracellular matrix , context (archaeology) , actin cytoskeleton , actin , cytoskeleton , signal transduction , biochemistry , cell , paleontology
Vinexin, CAP and 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 analyzed their functions in an identical cell context. Both vinexin α and CAP colocalized with vinculin at FAs and promoted the appearance of vinculin-rich FAs, whereas ArgBP2 colocalized with α-actinin at the proximal end of FAs and punctate structures on actin stress fibers (SFs), and induced paxillin-rich FAs. Furthermore, both vinexin α and CAP contributed to extracellular matrix stiffness-dependent vinculin behaviors, while ArgBP2 stabilized α-actinin on SFs and enhanced intracellular contractile forces. These results demonstrate the differential roles of SORBS proteins in mechanotransduction.