Carboxy-terminal modulator protein induces Akt phosphorylation and activation, thereby enhancing antiapoptotic, glycogen synthetic, and glucose uptake pathways.

Carboxy-terminal modulator protein induces Akt phosphorylation and activation, thereby enhancing antiapoptotic, glycogen synthetic, and glucose uptake pathways. Research Abstract Details 

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Carboxy-terminal modulator protein induces Akt phosphorylation and activation, thereby enhancing antiapoptotic, glycogen synthetic, and glucose uptake pathways. Abstract Text:

Hiraku Ono,Hideyuki Sakoda,Midori Fujishiro,Motonobu Anai,Akifumi Kushiyama,Yasushi Fukushima,Hideki Katagiri,Takehide Ogihara,Yoshitomo Oka,Hideaki Kamata,Nanao Horike,Yasunobu Uchijima,Hiroki Kurihara,Tomoichiro Asano,Hiraku Ono,Hideyuki Sakoda,Midori Fujishiro,Motonobu Anai,Akifumi Kushiyama,Yasushi Fukushima,Hideki Katagiri,Takehide Ogihara,Yoshitomo Oka,Hideaki Kamata,Nanao Horike,Yasunobu Uchijima,Hiroki Kurihara,Tomoichiro Asano,

Carboxy-terminal modulator protein (CTMP) was identified as binding to the carboxy terminus of Akt and inhibiting the phosphorylation and activation of Akt. In contrast to a previous study, we found CTMP overexpression to significantly enhance Akt phosphorylation at both Thr(308) and Ser(473) as well as the kinase activity of Akt, while phosphatidylinositol 3-kinase (PI3-kinase) activity was unaffected. Translocation of Akt to the membrane fraction was also markedly increased in response to overexpression of CTMP, with no change in the whole cellular content of Akt. Furthermore, the phosphorylations of GSK-3beta and Foxo1, well-known substrates of Akt, were increased by CTMP overexpression. On the other hand, suppression of CTMP with small interfering RNA partially but significantly attenuated this Akt phosphorylation. The cellular activities reportedly mediated by Akt activation were also enhanced by CTMP overexpression. UV-B-induced apoptosis of HeLa cells was significantly reversed not only by overexpression of the active mutant of Akt (myr-Akt) but also by that of CTMP. Increases in glucose transport activity and glycogen synthesis were also induced by overexpression of either myr-Akt or CTMP in 3T3-L1 adipocytes. Taking these results into consideration, it can be concluded that CTMP induces translocation of Akt to the membrane and thereby increases the level of Akt phosphorylation. As a result, CTMP enhances various cellular activities that are principally mediated by the PI3-kinase/Akt pathway.

Carboxy-terminal modulator protein induces Akt phosphorylation and activation, thereby enhancing antiapoptotic, glycogen synthetic, and glucose uptake pathways. Publishing Authors By Initials

H Ono,H Sakoda,M Fujishiro,M Anai,A Kushiyama,Y Fukushima,H Katagiri,T Ogihara,Y Oka,H Kamata,N Horike,Y Uchijima,H Kurihara,T Asano,H Ono,H Sakoda,M Fujishiro,M Anai,A Kushiyama,Y Fukushima,H Katagiri,T Ogihara,Y Oka,H Kamata,N Horike,Y Uchijima,H Kurihara,T Asano,

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Carboxy-terminal modulator protein induces Akt phosphorylation and activation, thereby enhancing antiapoptotic, glycogen synthetic, and glucose uptake pathways. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: American journal of physiology. Cell physiology

VOLUME: 293

Page Numbers: C1576-85

Journal Abbreviation: Am. J. Physiol., Cell Physiol.

ISSN: 0363-6143

DAY: 5

MONTH: 07

YEAR: 2007

Carboxy-terminal modulator protein induces Akt phosphorylation and activation, thereby enhancing antiapoptotic, glycogen synthetic, and glucose uptake pathways. Information

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LANGUAGE: eng

NlmUniqueID: 100901225

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Grant and Affiliation Information for Carboxy-terminal modulator protein induces Akt phosphorylation and activation, thereby enhancing antiapoptotic, glycogen synthetic, and glucose uptake pathways.

AFFILIATION: Department of Endocrinology and Metabolism, Institute for Adult Disease, Asahi Life Foundation, Tokyo.

Country: United States

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MEDLINETA: Am J Physiol Cell Physiol

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