Allosteric Regulation of PKM2 Allows Cellular Adaptation to Different Physiological States
Allosteric Regulation of PKM2 Allows Cellular Adaptation to Different Physiological States
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DOI：
10.1126/scisignal.2003925
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发表时间：
2013-02-19
影响因子：
7.3
通讯作者：
Vander Heiden, Matthew G.
中科院分区：
文献类型：
--
作者：
Gui, Dan Y.;Lewis, Caroline A.;Vander Heiden, Matthew G.
丙酮酸激酶亚型M2（PKM 2）活性受到复杂的变构调节。最近，丝氨酸和SAICAR（琥珀酰氨基咪唑甲酰胺核糖-5 '-磷酸）被鉴定为以前未被识别的PKM 2激活剂。这些发现增加了PKM 2在细胞中如何调节的额外复杂性，并支持调节PKM 2活性使细胞能够使其代谢状态适应特定生理环境的观点。
Pyruvate kinase isoform M2 (PKM2) activity is subject to complex allosteric regulation. Recently, serine and SAICAR (succinylaminoimidazolecarboxamide ribose-5'-phosphate) were identified as previously unrecognized activators of PKM2. These findings add additional complexity to how PKM2 is regulated in cells and support the notion that modulating PKM2 activity enables cells to adapt their metabolic state to specific physiological contexts.