[HTML][HTML] Phosphorylation and dimerization regulate nucleocytoplasmic shuttling of mammalian STE20-like kinase (MST)
KK Lee, S Yonehara - Journal of Biological Chemistry, 2002 - ASBMB
Mammalian STE20-like kinase (MST) is a member of the yeast STE20-related kinase family
and proteolytically activated by caspase during apoptosis. However, its other cellular
functions are not known, including its activation mechanism, substrate (s), and subcellular
localization. In this report, using anti-MST monoclonal antibodies, we clearly show that
endogenous MST is localized in cytoplasm in a leptomycin B-dependent manner. Analyses
with serial deletions and point mutations show that MST has two functional nuclear export …
and proteolytically activated by caspase during apoptosis. However, its other cellular
functions are not known, including its activation mechanism, substrate (s), and subcellular
localization. In this report, using anti-MST monoclonal antibodies, we clearly show that
endogenous MST is localized in cytoplasm in a leptomycin B-dependent manner. Analyses
with serial deletions and point mutations show that MST has two functional nuclear export …