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Serine‐threonine kinase receptor‐associated protein (STRAP) activates B‐myb function through direct interaction
Author(s) -
Ha Hyunjung,
Seong HyunA,
Manoharan Ravi
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.543.2
Serine‐threonine kinase receptor‐associated protein (STRAP), a TGF‐β receptor interacting protein, plays a role in various cellular responses, including cell growth, apoptosis, tumorigenesis, and development. In the present study, we report that STRAP physically interacts with B‐myb, and this interaction is mediated by three carboxyl‐terminal WD40 repeats of STRAP. Ectopic expression of STRAP enhances B‐myb transcriptional activity in a dose‐dependent manner by stimulating the nuclear translocation of B‐myb. Knockdown of endogenous STRAP results in a significant down‐regulation of B‐myb targets, such as cyclin D1, B‐myb, and clusterin. Functional analysis shows that STRAP potentiates B‐myb‐mediated suppression of zinc finger like protein 9 (ZPR9)‐induced apoptosis in a dose‐dependent manner through direct interaction. These results suggest STRAP may function as a positive regulator of B‐myb transcription factor.