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Ribosomal Protein S6 Kinase, 90-kd, 1 OKDB#: 2323
 Symbols: RPS6KA1 Species: human
 Synonyms: RIBOSOMAL S6 KINASE 1, RSK1|  Locus: 3 in Homo sapiens


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General Comment The RSK (ribosomal S6 kinase) family comprises growth factor-regulated serine/threonine kinases, known also as p90(rsk). In humans, the RSK family contains 3 closely regulated members: RSK1 (RPS6KA1; 601684), RSK2, and RSK3 (RPS6KA2; 601685). The highly conserved feature of all members of the RSK family is the presence of 2 nonidentical kinase catalytic domains. RSKs are implicated in the activation of the mitogen-activated kinase cascade (see OMIM 176872) and the stimulation of cell proliferation (at the transition between phases G0 and G1 of the cell cycle) and differentiation.

General function Cytoskeleton, Microtubule binding, Cytoskeleton organization
Comment
Cellular localization Nuclear
Comment
Ovarian function Oogenesis
Comment Characterization of ribosomal S6 protein kinase p90rsk during meiotic maturation and fertilization in pig oocytes: mitogen-activated protein kinase-associated activation and localization Fan HY, et al . Mitogen-activated protein kinase (MAPK) becomes activated during the meiotic maturation of pig oocytes, but its physiological substrate is unknown. The 90-kDa ribosome S6 protein kinase (p90rsk) is the best known MAPK substrate in Xenopus and mouse oocytes. The present study was designed to investigate the expression, phosphorylation, subcellular localization, and possible roles of p90rsk in porcine oocytes during meiotic maturation, fertilization, and parthenogenetic activation. This kinase was partially phosphorylated in oocytes at germinal vesicle (GV) stage through a MAPK-independent mechanism, but its full phosphorylation is dependent on MAPK activity. After fertilization or electrical activation, p90rsk was dephosphorylated shortly before pronucleus formation, which coincided with the inactivation of MAPK. A protein phosphatase inhibitor, okadaic acid, accelerated the phosphorylation of p90rsk during meiotic maturation and induced its rephosphorylation in activated eggs. MAPK kinase (MAPKK or MEK) inhibitor U0126 inhibited the activation of MAPK and p90rsk in both cumulus-enclosed and denuded pig oocytes, but prevented GV breakdown (GVBD) only in cumulus-enclosed oocytes. Active MAPK and p90rsk were detected in pig cumulus cells, and U0126 induced their dephosphorylation. In meiosis II arrested eggs, U0126 led to the inactivation of MAPK and p90rsk, as well as the interphase transition of the eggs. P90rsk was distributed evenly in GV oocytes, but it accumulated in the nucleus before GVBD. It was localized to the meiotic spindle after GVBD and concentrated in the spindle mid zone during emission of the polar bodies. All these results suggest that p90rsk is downstream of MAPK and plays functional roles in the regulation of nuclear status and microtubule organization. Although MAPK and p90rsk activity are not essential for the spontaneous meiotic resumption in denuded oocytes, activation of this cascade in cumulus cells is indispensable for the gonadotropin-induced meiotic resumption of pig oocytes.
Expression regulated by
Comment
Ovarian localization Oocyte, Cumulus
Comment
Follicle stages Antral, Preovulatory
Comment
Phenotypes
Mutations 0 mutations
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created: Jan. 2, 2004, 1 p.m. by: hsueh   email:
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last update: Jan. 2, 2004, 1:02 p.m. by: system    email:



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