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首页> 外文期刊>Cell cycle >Serine79-phosphorylated acetyl-CoA carboxylase, a downstream target of AMPK, localizes to the mitotic spindle poles and the cytokinesis furrow
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Serine79-phosphorylated acetyl-CoA carboxylase, a downstream target of AMPK, localizes to the mitotic spindle poles and the cytokinesis furrow

机译：丝氨酸79磷酸化的乙酰辅酶A羧化酶，AMPK的下游目标，定位于有丝分裂纺锤体极和胞质分裂

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摘要

Acetyl-CoA carboxylase (ACACA) is the rate-limiting enzyme in the biogenesis of long-chain fatty acids. Previous studies in yeast have shown that disruption of the ACACA gene impairs nuclear division, with ACACA-de￡e.ctive yeast cells developing large undivided nuclei and showing abnormally shortened mitotic spindles that lastly result in aberrant mitosis and cell cycle arrest at G_2/M; these findings suggested that ACACA might have an essential role in the progression of cell division. Moreover, the addition of a mixture of long-chain fatty acids, the final product of the endogenous fatty acid synthesis, failed to overcome the cell cycle arrest, additionally suggesting that the role of ACACA in cell division may be independent of its well-recognized biosynthetic function or, alternatively, an strict coupling between lipogenesis and cell cycle progression
机译：乙酰辅酶A羧化酶（ACACA）是长链脂肪酸生物合成中的限速酶。先前在酵母中的研究表明，ACACA基因的破坏会破坏核分裂，伴随ACACA活性的酵母细胞发育出大的未分裂核，并显示出异常缩短的有丝分裂纺锤体，最终导致异常的有丝分裂和细胞周期停滞在G_2 / M ;这些发现表明ACACA可能在细胞分裂的进程中起着至关重要的作用。此外，添加长链脂肪酸的混合物（内源性脂肪酸合成的最终产物）无法克服细胞周期停滞现象，另外表明ACACA在细胞分裂中的作用可能与其公认的独立生物合成功能，或脂肪生成与细胞周期进程之间的严格耦合

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