Myosin phosphatase dephosphorylates HDAC7, controls its nucleocytoplasmic shuttling, and inhibits apoptosis in thymocytes.

The repressive activity of histone deacetylase 7 (HDAC7), a class IIa HDAC expressed in CD4+CD8+ double-positive thymocytes, is regulated by its nucleocytoplasmic shuttling. In resting thymocytes, HDAC7 is nuclear and functions as a transcriptional repressor. After T-cell receptor (TCR) activation, the serine/threonine kinase PKD1 phosphorylates HDAC7, resulting in its nuclear ...
export and the derepression of its target genes. Here, we identify protein phosphatase 1beta (PP1beta) and myosin phosphatase targeting subunit 1 (MYPT1), two components of the myosin phosphatase complex, as HDAC7-associated proteins in thymocytes. Myosin phosphatase dephosphorylates HDAC7 and promotes its nuclear localization, leading to the repression of the HDAC7 target, Nur77, and the inhibition of apoptosis in CD4+CD8+ thymocytes.
Mesh Terms:
Active Transport, Cell Nucleus, Animals, Apoptosis, Cell Line, DNA-Binding Proteins, Histone Deacetylases, Mice, Mice, Inbred BALB C, Myosin-Light-Chain Kinase, Myosin-Light-Chain Phosphatase, Nuclear Receptor Subfamily 4, Group A, Member 1, Phosphoprotein Phosphatases, Phosphorylation, Protein Phosphatase 1, RNA, Small Interfering, Receptors, Antigen, T-Cell, Receptors, Cytoplasmic and Nuclear, Receptors, Steroid, Recombinant Proteins, T-Lymphocytes, Tetradecanoylphorbol Acetate, Transcription Factors
Genes Dev.
Date: Mar. 15, 2007
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