Intracellular Signaling by Akt: Bound to Be Specific
Intracellular Signaling by Akt: Bound to Be Specific
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DOI：
10.1126/scisignal.124pe29
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发表时间：
2008-06-17
影响因子：
7.3
通讯作者：
Franke, Thomas F.
中科院分区：
文献类型：
--
作者：
Franke, Thomas F.
在过去的十年里，丝氨酸/苏氨酸激酶Akt(也被称为蛋白激酶B)已经成为真核细胞中的一个关键信号分子。除了阐明上游激酶和磷酸酶对其调控所需的研究外，在确定Akt结合伙伴方面也取得了进展，这些伙伴调节其激活，调节其激酶活性，并确定其对下游生物反应的影响。对Akt结合分子的研究突出了参与调节激活的肌醇磷脂3-激酶下游信号的新机制。AKT相互作用的分子在生理和病理条件下都可能在Akt信号转导中发挥重要作用。
Over the past decade, the serine/threonine kinase Akt (also known as protein kinase B) has emerged as a critical signaling molecule within eukaryotic cells. In addition to the research required for the clarification of its regulation by upstream kinases and phosphatases, progress has been made in the identification of Akt-binding partners that modulate its activation, regulate its kinase activity, and define its impact on downstream biological responses. Studies of Akt-binding molecules have highlighted novel mechanisms involved in the regulation of signaling downstream of activated phosphoinositide 3-kinase. Akt-interacting molecules may have important roles in Akt signal transduction both under physiological and pathological conditions.