Abstract
The reversible phosphorylation of proteins controlled by protein kinases and protein phosphatases is a major mechanism that regulates a wide variety of cellular processes. In contrast to C. elegans, recent studies in mammalian cells have highlighted a major role of serine/threonine protein phosphorylation in apoptosis. To illustrate the importance of dephosphorylation processes in apoptosis, this review will focus on recent studies suggesting that the interaction of the serine/threonine protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) with certain regulators of the Bcl-2 family is critically involved in the control of apoptosis.
Publication types
-
Research Support, Non-U.S. Gov't
-
Review
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Apoptosis / physiology*
-
Carrier Proteins / metabolism
-
Cell Survival / physiology
-
Humans
-
Molecular Sequence Data
-
Phosphatidylinositol 3-Kinases / metabolism
-
Phosphoprotein Phosphatases / metabolism*
-
Phosphorylation
-
Protein Phosphatase 1
-
Protein Phosphatase 2
-
Protein Serine-Threonine Kinases*
-
Proto-Oncogene Proteins / metabolism
-
Proto-Oncogene Proteins c-akt
-
Proto-Oncogene Proteins c-bcl-2 / metabolism
-
bcl-Associated Death Protein
Substances
-
BAD protein, human
-
Carrier Proteins
-
Proto-Oncogene Proteins
-
Proto-Oncogene Proteins c-bcl-2
-
bcl-Associated Death Protein
-
Protein Serine-Threonine Kinases
-
Proto-Oncogene Proteins c-akt
-
Phosphoprotein Phosphatases
-
Protein Phosphatase 1
-
Protein Phosphatase 2