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Рибосомный белок киназы S6, полипептид 1 70kDa
	; Представлено на основе PDB 3A60.
Доступные структуры
PDB	Поиск ортологов: PDBe, RCSB
Список идентификаторов PDB
	3A60, 3A61, 3A62, 4L3J, 4L3L, 4L42, 4L43, 4L44, 4L45, 4L46
Идентификаторы
Символ	RPS6KB1 ; PS6K; S6K; S6K-beta-1; S6K1; STK14A; p70 S6KA; p70(S6K)-alpha; p70-S6K; p70-alpha
Внешние ID	OMIM: 608938 HomoloGene: 81703 IUPHAR: ChEMBL: 4501 GeneCards: RPS6KB1 Gene
номер EC	2.7.11.1
Генная онтология
Функция	• protein kinase activity; • ribosomal protein S6 kinase activity; • protein serine/threonine/tyrosine kinase activity; • protein binding; • ATP binding; • peptide binding;
Компонент клетки	• nucleus; • nucleolus; • cytoplasm; • mitochondrion; • mitochondrial outer membrane; • cytosol; • cell surface; • cell junction; • neuron projection; • synapse; • perinuclear region of cytoplasm;
Биологический процесс	• G1/S transition of mitotic cell cycle; • skeletal muscle contraction; • protein phosphorylation; • apoptotic process; • signal transduction; • germ cell development; • aging; • response to nutrient; • long-term memory; • insulin receptor signaling pathway; • response to heat; • response to wounding; • response to mechanical stimulus; • response to toxic substance; • response to glucose; • skeletal muscle atrophy; • response to electrical stimulus involved in regulation of muscle adaptation; • positive regulation of smooth muscle cell migration; • cell migration; • TOR signaling; • response to lipopolysaccharide; • response to testosterone; • response to glucagon; • response to tumor necrosis factor; • response to drug; • negative regulation of apoptotic process; • response to leucine; • protein kinase B signaling; • response to ethanol; • positive regulation of translation; • positive regulation of mitotic cell cycle; • positive regulation of translational initiation; • regulation of glucose import; • negative regulation of insulin receptor signaling pathway; • phosphatidylinositol-mediated signaling; • positive regulation of skeletal muscle tissue growth; • positive regulation of smooth muscle cell proliferation; • response to glucocorticoid; • cellular response to growth factor stimulus; • negative regulation of extrinsic apoptotic signaling pathway;
	Источники: Amigo / QuickGO
Профиль экспрессии РНК
	Больше информации
Ортологи
	Шаблон: просмотр • обсуждение • править

ПОИСК ПО САЙТУ | о проекте

Рибосомальная протеинкиназа S6 бета-1 — фермент, кодируемый у человека геном RPS6KB1 .^[1]^[2]

Функция

Этот ген кодирует члена RSK^[en] (рибосомной S6 киназы) семейства серин/треониновых киназ^[en]. Эта киназа фосфорилирует несколько остатков рибосомального белка S6^[en]. Киназы этого белка приводит к увеличению синтеза белка и пролиферации клеток.

Клиническое значение

Ингибирование белка S6K1, или его отсутствие, замедляет производство жировых клеток, нарушая и замедляя начальную стадию их образования. Исследование может иметь значение для лечения ожирения.^[3]

Усиление в области ДНК, кодируемый этим геном и сверхэкспрессия этой киназы видны в некоторых клеточных линиях рака молочной железы.

Другой путь, в котором участвует P70, мышечное удлинение и рост. P70 фосфорилируется пассивно при напряжении камбаловидной мышцы. Она может быть одной из многих протеинкиназ, участвующих в мышечной ткани.^[4]

Взаимодействия

P70-S6 киназы 1, как было выявлено, взаимодействует с:

COASY,^[5]
CSNK2B,^[6]
EIF3B,^[7]
KIAA1303,^[8]^[9]^[10]^[11]
MTOR,^[12]^[13]^[14]^[15]^[16]^[17]^[18]^[19]^[20]^[21]^[22]^[23]
POLDIP3,^[24]
PPP2R2A,^[25]^[26]
RBX1,^[27] и
UBC^[en].^[27]

Примечания

↑ Grove JR, Banerjee P, Balasubramanyam A, Coffer PJ, Price DJ, Avruch J, Woodgett JR (1991). “Cloning and expression of two human p70 S6 kinase polypeptides differing only at their amino termini”. Mol Cell Biol. 11 (11): 5541—50. PMC 361924. PMID 1922062.
↑ Entrez Gene: RPS6KB1 ribosomal protein S6 kinase, 70kDa, polypeptide 1 (неопр.).
↑ Carnevalli, L; NCarnevalli LS, Masuda K, Frigerio F, Le Bacquer O, Um SH, Gandin V, Topisirovic I, Sonenberg N, Thomas G, Kozma SC (2010). “S6K1 Plays a Critical Role in Early Adipocyte Differentiation”. Dev Cell. 18 (5): 763—74. DOI:10.1016/j.devcel.2010.02.018. PMC 2918254. PMID 20493810. Используется устаревший параметр |coauthors= (справка)
↑ Van Dyke JM, Bain JL, Riley DA (April 2013). “Stretch activated signaling is modulated by stretch magnitude and contraction”. Muscle Nerve. 49 (1): 98—107. DOI:10.1002/mus.23880. PMID 23620271.
↑ Nemazanyy I, Panasyuk G, Zhyvoloup A, Panayotou G, Gout IT, Filonenko V (2004). “Specific interaction between S6K1 and CoA synthase: a potential link between the mTOR/S6K pathway, CoA biosynthesis and energy metabolism”. FEBS Lett. 578 (3): 357—62. DOI:10.1016/j.febslet.2004.10.091. PMID 15589845.
↑ Panasyuk G, Nemazanyy I, Zhyvoloup A, Bretner M, Litchfield DW, Filonenko V, Gout IT (2006). “Nuclear export of S6K1 II is regulated by protein kinase CK2 phosphorylation at Ser-17”. J. Biol. Chem. 281 (42): 31188—201. DOI:10.1074/jbc.M602618200. PMID 16895915.
↑ Holz MK, Ballif BA, Gygi SP, Blenis J (2005). “mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events”. Cell. 123 (4): 569—80. DOI:10.1016/j.cell.2005.10.024. PMID 16286006.
↑ Ali SM, Sabatini DM (2005). “Structure of S6 kinase 1 determines whether raptor-mTOR or rictor-mTOR phosphorylates its hydrophobic motif site”. J. Biol. Chem. 280 (20): 19445—8. DOI:10.1074/jbc.C500125200. PMID 15809305.
↑ Ha SH, Kim DH, Kim IS, Kim JH, Lee MN, Lee HJ, Kim JH, Jang SK, Suh PG, Ryu SH (2006). “PLD2 forms a functional complex with mTOR/raptor to transduce mitogenic signals”. Cell. Signal. 18 (12): 2283—91. DOI:10.1016/j.cellsig.2006.05.021. PMID 16837165.
↑ Hara K, Maruki Y, Long X, Yoshino K, Oshiro N, Hidayat S, Tokunaga C, Avruch J, Yonezawa K (2002). “Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action”. Cell. 110 (2): 177—89. DOI:10.1016/S0092-8674(02)00833-4. PMID 12150926.
↑ Nojima H, Tokunaga C, Eguchi S, Oshiro N, Hidayat S, Yoshino K, Hara K, Tanaka N, Avruch J, Yonezawa K (2003). “The mammalian target of rapamycin (mTOR) partner, raptor, binds the mTOR substrates p70 S6 kinase and 4E-BP1 through their TOR signaling (TOS) motif”. J. Biol. Chem. 278 (18): 15461—4. DOI:10.1074/jbc.C200665200. PMID 12604610.
↑ Chiang GG, Abraham RT (2005). “Phosphorylation of mammalian target of rapamycin (mTOR) at Ser-2448 is mediated by p70S6 kinase”. J. Biol. Chem. 280 (27): 25485—90. DOI:10.1074/jbc.M501707200. PMID 15899889.
↑ Holz MK, Blenis J (2005). “Identification of S6 kinase 1 as a novel mammalian target of rapamycin (mTOR)-phosphorylating kinase”. J. Biol. Chem. 280 (28): 26089—93. DOI:10.1074/jbc.M504045200. PMID 15905173.
↑ Isotani S, Hara K, Tokunaga C, Inoue H, Avruch J, Yonezawa K (1999). “Immunopurified mammalian target of rapamycin phosphorylates and activates p70 S6 kinase alpha in vitro”. J. Biol. Chem. 274 (48): 34493—8. DOI:10.1074/jbc.274.48.34493. PMID 10567431.
↑ Long X, Lin Y, Ortiz-Vega S, Yonezawa K, Avruch J (2005). “Rheb binds and regulates the mTOR kinase”. Curr. Biol. 15 (8): 702—13. DOI:10.1016/j.cub.2005.02.053. PMID 15854902.
↑ Toral-Barza L, Zhang WG, Lamison C, Larocque J, Gibbons J, Yu K (2005). “Characterization of the cloned full-length and a truncated human target of rapamycin: activity, specificity, and enzyme inhibition as studied by a high capacity assay”. Biochem. Biophys. Res. Commun. 332 (1): 304—10. DOI:10.1016/j.bbrc.2005.04.117. PMID 15896331.
↑ Saitoh M, Pullen N, Brennan P, Cantrell D, Dennis PB, Thomas G (2002). “Regulation of an activated S6 kinase 1 variant reveals a novel mammalian target of rapamycin phosphorylation site”. J. Biol. Chem. 277 (22): 20104—12. DOI:10.1074/jbc.M201745200. PMID 11914378.
↑ Kim DH, Sarbassov DD, Ali SM, King JE, Latek RR, Erdjument-Bromage H, Tempst P, Sabatini DM (2002). “mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery”. Cell. 110 (2): 163—75. DOI:10.1016/S0092-8674(02)00808-5. PMID 12150925.
↑ Edinger AL, Linardic CM, Chiang GG, Thompson CB, Abraham RT (2003). “Differential effects of rapamycin on mammalian target of rapamycin signaling functions in mammalian cells”. Cancer Res. 63 (23): 8451—60. PMID 14679009.
↑ Leone M, Crowell KJ, Chen J, Jung D, Chiang GG, Sareth S, Abraham RT, Pellecchia M (2006). “The FRB domain of mTOR: NMR solution structure and inhibitor design”. Biochemistry. 45 (34): 10294—302. DOI:10.1021/bi060976+. PMID 16922504.
↑ Takahashi T, Hara K, Inoue H, Kawa Y, Tokunaga C, Hidayat S, Yoshino K, Kuroda Y, Yonezawa K (2000). “Carboxyl-terminal region conserved among phosphoinositide-kinase-related kinases is indispensable for mTOR function in vivo and in vitro”. Genes Cells. 5 (9): 765—75. DOI:10.1046/j.1365-2443.2000.00365.x. PMID 10971657.
↑ Burnett PE, Barrow RK, Cohen NA, Snyder SH, Sabatini DM (1998). “RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1”. Proc. Natl. Acad. Sci. U.S.A. 95 (4): 1432—7. DOI:10.1073/pnas.95.4.1432. PMC 19032. PMID 9465032.
↑ Sarbassov DD, Sabatini DM (2005). “Redox regulation of the nutrient-sensitive raptor-mTOR pathway and complex”. J. Biol. Chem. 280 (47): 39505—9. DOI:10.1074/jbc.M506096200. PMID 16183647.
↑ Richardson CJ, Bröenstrup M, Fingar DC, Jülich K, Ballif BA, Gygi S, Blenis J (2004). “SKAR is a specific target of S6 kinase 1 in cell growth control”. Curr. Biol. 14 (17): 1540—9. DOI:10.1016/j.cub.2004.08.061. PMID 15341740.
↑ Peterson RT, Desai BN, Hardwick JS, Schreiber SL (1999). “Protein phosphatase 2A interacts with the 70-kDa S6 kinase and is activated by inhibition of FKBP12-rapamycinassociated protein”. Proc. Natl. Acad. Sci. U.S.A. 96 (8): 4438—42. DOI:10.1073/pnas.96.8.4438. PMC 16350. PMID 10200280.
↑ Bishop JD, Nien WL, Dauphinee SM, Too CK (2006). “Prolactin activates mammalian target-of-rapamycin through phosphatidylinositol 3-kinase and stimulates phosphorylation of p70S6K and 4E-binding protein-1 in lymphoma cells”. J. Endocrinol. 190 (2): 307—12. DOI:10.1677/joe.1.06368. PMID 16899564.
1 2 Panasyuk G, Nemazanyy I, Filonenko V, Gout I (2008). “Ribosomal protein S6 kinase 1 interacts with and is ubiquitinated by ubiquitin ligase ROC1”. Biochem. Biophys. Res. Commun. 369 (2): 339—43. DOI:10.1016/j.bbrc.2008.02.016. PMID 18279656.

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[pmid1922062-1] Grove JR, Banerjee P, Balasubramanyam A, Coffer PJ, Price DJ, Avruch J, Woodgett JR (1991). “Cloning and expression of two human p70 S6 kinase polypeptides differing only at their amino termini”. Mol Cell Biol. 11 (11): 5541—50. PMC 361924. PMID 1922062.

[entrez-2] Entrez Gene: RPS6KB1 ribosomal protein S6 kinase, 70kDa, polypeptide 1 (неопр.).

[pmid_20493810-3] Carnevalli, L; NCarnevalli LS, Masuda K, Frigerio F, Le Bacquer O, Um SH, Gandin V, Topisirovic I, Sonenberg N, Thomas G, Kozma SC (2010). “S6K1 Plays a Critical Role in Early Adipocyte Differentiation”. Dev Cell. 18 (5): 763—74. DOI:10.1016/j.devcel.2010.02.018. PMC 2918254. PMID 20493810. Используется устаревший параметр |coauthors= (справка)

[pmid23620271-4] Van Dyke JM, Bain JL, Riley DA (April 2013). “Stretch activated signaling is modulated by stretch magnitude and contraction”. Muscle Nerve. 49 (1): 98—107. DOI:10.1002/mus.23880. PMID 23620271.

[pmid15589845-5] Nemazanyy I, Panasyuk G, Zhyvoloup A, Panayotou G, Gout IT, Filonenko V (2004). “Specific interaction between S6K1 and CoA synthase: a potential link between the mTOR/S6K pathway, CoA biosynthesis and energy metabolism”. FEBS Lett. 578 (3): 357—62. DOI:10.1016/j.febslet.2004.10.091. PMID 15589845.

[pmid16895915-6] Panasyuk G, Nemazanyy I, Zhyvoloup A, Bretner M, Litchfield DW, Filonenko V, Gout IT (2006). “Nuclear export of S6K1 II is regulated by protein kinase CK2 phosphorylation at Ser-17”. J. Biol. Chem. 281 (42): 31188—201. DOI:10.1074/jbc.M602618200. PMID 16895915.

[pmid16286006-7] Holz MK, Ballif BA, Gygi SP, Blenis J (2005). “mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events”. Cell. 123 (4): 569—80. DOI:10.1016/j.cell.2005.10.024. PMID 16286006.

[pmid15809305-8] Ali SM, Sabatini DM (2005). “Structure of S6 kinase 1 determines whether raptor-mTOR or rictor-mTOR phosphorylates its hydrophobic motif site”. J. Biol. Chem. 280 (20): 19445—8. DOI:10.1074/jbc.C500125200. PMID 15809305.

[pmid16837165-9] Ha SH, Kim DH, Kim IS, Kim JH, Lee MN, Lee HJ, Kim JH, Jang SK, Suh PG, Ryu SH (2006). “PLD2 forms a functional complex with mTOR/raptor to transduce mitogenic signals”. Cell. Signal. 18 (12): 2283—91. DOI:10.1016/j.cellsig.2006.05.021. PMID 16837165.

[pmid12150926-10] Hara K, Maruki Y, Long X, Yoshino K, Oshiro N, Hidayat S, Tokunaga C, Avruch J, Yonezawa K (2002). “Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action”. Cell. 110 (2): 177—89. DOI:10.1016/S0092-8674(02)00833-4. PMID 12150926.

[pmid12604610-11] Nojima H, Tokunaga C, Eguchi S, Oshiro N, Hidayat S, Yoshino K, Hara K, Tanaka N, Avruch J, Yonezawa K (2003). “The mammalian target of rapamycin (mTOR) partner, raptor, binds the mTOR substrates p70 S6 kinase and 4E-BP1 through their TOR signaling (TOS) motif”. J. Biol. Chem. 278 (18): 15461—4. DOI:10.1074/jbc.C200665200. PMID 12604610.

[pmid15899889-12] Chiang GG, Abraham RT (2005). “Phosphorylation of mammalian target of rapamycin (mTOR) at Ser-2448 is mediated by p70S6 kinase”. J. Biol. Chem. 280 (27): 25485—90. DOI:10.1074/jbc.M501707200. PMID 15899889.

[pmid15905173-13] Holz MK, Blenis J (2005). “Identification of S6 kinase 1 as a novel mammalian target of rapamycin (mTOR)-phosphorylating kinase”. J. Biol. Chem. 280 (28): 26089—93. DOI:10.1074/jbc.M504045200. PMID 15905173.

[pmid10567431-14] Isotani S, Hara K, Tokunaga C, Inoue H, Avruch J, Yonezawa K (1999). “Immunopurified mammalian target of rapamycin phosphorylates and activates p70 S6 kinase alpha in vitro”. J. Biol. Chem. 274 (48): 34493—8. DOI:10.1074/jbc.274.48.34493. PMID 10567431.

[pmid15854902-15] Long X, Lin Y, Ortiz-Vega S, Yonezawa K, Avruch J (2005). “Rheb binds and regulates the mTOR kinase”. Curr. Biol. 15 (8): 702—13. DOI:10.1016/j.cub.2005.02.053. PMID 15854902.

[pmid15896331-16] Toral-Barza L, Zhang WG, Lamison C, Larocque J, Gibbons J, Yu K (2005). “Characterization of the cloned full-length and a truncated human target of rapamycin: activity, specificity, and enzyme inhibition as studied by a high capacity assay”. Biochem. Biophys. Res. Commun. 332 (1): 304—10. DOI:10.1016/j.bbrc.2005.04.117. PMID 15896331.

[pmid11914378-17] Saitoh M, Pullen N, Brennan P, Cantrell D, Dennis PB, Thomas G (2002). “Regulation of an activated S6 kinase 1 variant reveals a novel mammalian target of rapamycin phosphorylation site”. J. Biol. Chem. 277 (22): 20104—12. DOI:10.1074/jbc.M201745200. PMID 11914378.

[pmid12150925-18] Kim DH, Sarbassov DD, Ali SM, King JE, Latek RR, Erdjument-Bromage H, Tempst P, Sabatini DM (2002). “mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery”. Cell. 110 (2): 163—75. DOI:10.1016/S0092-8674(02)00808-5. PMID 12150925.

[pmid14679009-19] Edinger AL, Linardic CM, Chiang GG, Thompson CB, Abraham RT (2003). “Differential effects of rapamycin on mammalian target of rapamycin signaling functions in mammalian cells”. Cancer Res. 63 (23): 8451—60. PMID 14679009.

[pmid16922504-20] Leone M, Crowell KJ, Chen J, Jung D, Chiang GG, Sareth S, Abraham RT, Pellecchia M (2006). “The FRB domain of mTOR: NMR solution structure and inhibitor design”. Biochemistry. 45 (34): 10294—302. DOI:10.1021/bi060976+. PMID 16922504.

[pmid10971657-21] Takahashi T, Hara K, Inoue H, Kawa Y, Tokunaga C, Hidayat S, Yoshino K, Kuroda Y, Yonezawa K (2000). “Carboxyl-terminal region conserved among phosphoinositide-kinase-related kinases is indispensable for mTOR function in vivo and in vitro”. Genes Cells. 5 (9): 765—75. DOI:10.1046/j.1365-2443.2000.00365.x. PMID 10971657.

[pmid9465032-22] Burnett PE, Barrow RK, Cohen NA, Snyder SH, Sabatini DM (1998). “RAFT1 phosphorylation of the translational regulators p70 S6 kinase and 4E-BP1”. Proc. Natl. Acad. Sci. U.S.A. 95 (4): 1432—7. DOI:10.1073/pnas.95.4.1432. PMC 19032. PMID 9465032.

[pmid16183647-23] Sarbassov DD, Sabatini DM (2005). “Redox regulation of the nutrient-sensitive raptor-mTOR pathway and complex”. J. Biol. Chem. 280 (47): 39505—9. DOI:10.1074/jbc.M506096200. PMID 16183647.

[pmid15341740-24] Richardson CJ, Bröenstrup M, Fingar DC, Jülich K, Ballif BA, Gygi S, Blenis J (2004). “SKAR is a specific target of S6 kinase 1 in cell growth control”. Curr. Biol. 14 (17): 1540—9. DOI:10.1016/j.cub.2004.08.061. PMID 15341740.

[pmid10200280-25] Peterson RT, Desai BN, Hardwick JS, Schreiber SL (1999). “Protein phosphatase 2A interacts with the 70-kDa S6 kinase and is activated by inhibition of FKBP12-rapamycinassociated protein”. Proc. Natl. Acad. Sci. U.S.A. 96 (8): 4438—42. DOI:10.1073/pnas.96.8.4438. PMC 16350. PMID 10200280.

[pmid16899564-26] Bishop JD, Nien WL, Dauphinee SM, Too CK (2006). “Prolactin activates mammalian target-of-rapamycin through phosphatidylinositol 3-kinase and stimulates phosphorylation of p70S6K and 4E-binding protein-1 in lymphoma cells”. J. Endocrinol. 190 (2): 307—12. DOI:10.1677/joe.1.06368. PMID 16899564.

[pmid18279656-27] 1 2 Panasyuk G, Nemazanyy I, Filonenko V, Gout I (2008). “Ribosomal protein S6 kinase 1 interacts with and is ubiquitinated by ubiquitin ligase ROC1”. Biochem. Biophys. Res. Commun. 369 (2): 339—43. DOI:10.1016/j.bbrc.2008.02.016. PMID 18279656.