[HTML][HTML] Bcl-2 Phosphorylation by p38 MAPK: identification of target sites and biologic consequences

G De Chiara, ME Marcocci, M Torcia… - Journal of biological …, 2006 - ASBMB
The antiapoptotic role of Bcl-2 can be regulated by its phosphorylation in serine and
threonine residues located in a nonstructured loop that links BH3 and BH4 domains. p38
MAPK has been identified as one of the kinases able to mediate such phosphorylation,
through direct interaction with Bcl-2 protein in the mitochondrial compartment. In this study,
we identify, by using mass spectrometry techniques and specific anti-phosphopeptide
antibodies, Ser 87 and Thr 56 as the Bcl-2 residues phosphorylated by p38 MAPK and show …