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Polo-like kinase 1 phosphorylates and regulates Bcl-xL during pironetin-induced apoptosis
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Polo-like kinase 1 phosphorylates and regulates Bcl-xL during pironetin-induced apoptosis
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Journal Article
Polo-like kinase 1 phosphorylates and regulates Bcl-xL during pironetin-induced apoptosis
2009
Overview
Bcl-x
L
, an anti-apoptotic Bcl-2 family member protein, contributes to the resistance against chemotherapies such as tubulin-binder treatment in many human tumors. Although Bcl-x
L
is phosphorylated after tubulin-binder treatment, the role of the phosphorylation and its responsible kinase(s) are poorly understood. Here, we identified Plk1 (polo-like kinase 1) as a Bcl-x
L
kinase. Same location of Bcl-x
L
and Plk1 was revealed by immunocytochemical analyses at M-phase
in situ
. Plk1 phosphorylates Bcl-x
L
in vitro
, and we identified Plk1 phosphorylation sites in Bcl-x
L
. When all of these phosphorylation sites were substituted to alanines, the anti-apoptotic activity of the Bcl-x
L
mutant against the apoptosis induced by pironetin, but not against ultraviolet-induced apoptosis, was increased. These observations suggest that Plk1 is a regulator of Bcl-x
L
phosphorylation and controls the anti-apoptotic activity of Bcl-x
L
during pironetin-induced apoptosis.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
