期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 101, 期 18, 页码 7187-7192出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0401673101
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资金
- NIDA NIH HHS [P01 DA010044, DA10044] Funding Source: Medline
- NIMH NIH HHS [P01 MH040899, MH40899] Funding Source: Medline
Protein phosphatase 1 (PP1) is a multifunctional enzyme with diverse roles in the nervous system, including regulation of synaptic activity and dendritic morphology. PP1 activity is controlled via association with a family of regulatory subunits that govern subcellular localization and substrate specificity. A previously un-described class of PP1-binding proteins was detected by interaction cloning. Family members were also found to bind to cytoplasmic actin via Arg, Pro, Glu, and Leu repeat-containing sequences. The prototypical member of this family, phosphatase and actin regulator (phactr) 1 was a potent modulator of PP1 activity in vitro. Phactr-1 protein is selectively expressed in brain, where high levels were found in cortex, hippocampus, and striatum, with enrichment of the protein at synapses. Additional family members displayed highly distinct mRNA transcript expression patterns within rat brain. The current findings present a mechanism by which PP1 may be directed toward neuronal substrates associated with the actin cytoskeleton.
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