Recruitment and activation of SLK at the leading edge of migrating cells requires Src family kinase activity and the LIM-only protein 4
Kyla D Baron, Khalid Al-Zahrani, Jillian Conway, Cedrik Labreche, Christopher J Storbeck, Jane E Visvader, Luc A Sabourin
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | ELSEVIER SCIENCE BV | Published : 2015
The Ste20-like kinase SLK plays a pivotal role in cell migration and focal adhesion turnover and is regulated by the LIM domain-binding proteins Ldb1 and Ldb2. These adapter proteins have been demonstrated to interact with LMO4 in the organization of transcriptional complexes. Therefore, we have assessed the ability of LMO4 to also interact and regulate SLK activity. Our data show that LMO4 can directly bind to SLK and activate its kinase activity in vitro and in vivo. LMO4 can be co-precipitated with SLK following the induction of cell migration by scratch wounding and Cre-mediated deletion of LMO4 in conditional LMO4(fl/fl) fibroblasts inhibits cell migration and SLK activation. Deletion o..View full abstract
KDB and KNA are recipients of a Canadian Breast Cancer Foundation - Ontario Region Doctoral Fellowship. This work was supported by the Canadian Institute of Health Research and the Canadian Breast Cancer Foundation.