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Protein phosphatase 1, catalytic subunit alpha OKDB#: 1091
 Symbols: Protein phosphatase 1, catalytic subunit alpha Species: human
 Synonyms: PROTEIN PHOSPHATASE 1, ALPHA SUBUNIT, PPP1A|  Locus: 11q13 in Homo sapiens


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General Comment Phosphorylation of serine and threonine residues in proteins is a crucial step in the regulation of many cellular functions ranging from hormonal regulation to cell division and even short-term memory. The level of phosphorylation is controlled by the opposing actions of protein kinases and protein phosphatases. Protein phosphatase 1 (PP1) is 1 of 4 major serine/threonine-specific protein phosphatases which have been identified in eukaryotic cells by enzymatic methods. Although the 4 have overlapping substrate specificities in vitro, they can be distinguished by the use of inhibitor proteins and by their dependence on metal ions. Type 1 protein phosphatases are inhibited by nanomolar concentrations of the thermostable proteins, inhibitor 1 and inhibitor 2, while the 3 type 2 protein phosphatases are unaffected.

General function Intracellular signaling cascade
Comment
Cellular localization Cytoplasmic
Comment
Ovarian function Luteinization
Comment
Expression regulated by
Comment
Ovarian localization Granulosa, Luteal cells
Comment
Follicle stages Preovulatory, Corpus luteum
Comment Mayerhofer A, et al 2001 reported the role of D1-Receptor, DARPP-32, and PP-1 in the Primate Corpus Luteum and Luteinized Granulosa Cells. The multifunctional phosphoprotein "dopamine and cAMP-related phosphoprotein, M(r) 32,000" (DARPP-32), which is able to act as an intracellular third messenger, was found to be present in human luteinized granulosa cells (GCs) and human ovary. DARPP-32 phosphorylation in GCs was increased by dopamine (DA) acting via a DA-1 receptors (D1-R). Immunoprecipitation studies showed that hCG, as well as DA, increased phosphorylation of DARPP-32 at threonine residues within 10 min, indicating that the signal transduction pathways of a hormone and a neurotransmitter involve DARPP-32 in GCs. Phosphorylated DARPP-32 is known to inhibit a cellular phosphatase (PP-1), which was also found to be expressed by GCs. Using RT-PCR and sequence analyses the authors showed that DARPP-32, PP-1, and D1-R genes were not restricted to cultured luteinized GCs, but were expressed in vivo, in the corpus luteum (CL) of the rhesus monkey throughout its entire life span. Although the precise role of D1-R in the CL remains to be shown, the presence of D1-R, DARPP-32, and its target PP-1 in this endocrine tissue, as well as the phosphorylation of DARPP-32 by a gonadotropin and by DA in luteinized GCs, indicate that the signal transduction pathways of the neurotransmitter DA and the gonadotropin hCG/LH involve DARPP-32. The PP-1 inhibitor DARPP-32 may, thus, be a third messenger used by both DA and hCG/LH to exert common regulatory influences on the cells of the CL.
Phenotypes
Mutations 0 mutations
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created: Jan. 18, 2001, 8:57 a.m. by: hsueh   email:
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last update: Aug. 14, 2001, 10:31 a.m. by: hsueh    email:



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