Vazquez-Martin Alejandro, López-Bonet Eugeni, Oliveras-Ferraros Cristina, Pérez-Martínez Maria Carmen, Bernadó Luis, Menendez Javier A
Cell Cycle. 2009 Mar 1;8(5):788-91. doi: 10.4161/cc.8.5.7787. Epub 2009 Mar 6.
When interrogating the activation status of AMP-activated protein kinase-measured as AMPKalpha(Thr172) phosphorylation-in tissue sections of human carcinomas and in cultured human cancer cells, the spatiotemporal dynamics of AMPK activity during the G(1)/S-to-M-phase transition strikingly resembles that of well-characterized "chromosomal passenger" proteins such as Aurora B, INCENP or Histone H3. The mitotic kinase behavior of the active form of AMPK may represent a candidate molecular link through which energy status directly influences tumorigenesis. A definitive elucidation of phospho-AMPKalpha(Thr172) in coordinating the chromosomal and cytoskeletal events of mitosis might radically amend our current perception of other AMPK-related diseases such as obesity, cardiac hypertrophy or accelerated aging syndromes.
在检测人癌组织切片和培养的人癌细胞中AMP激活的蛋白激酶的激活状态(以AMPKα(苏氨酸172)磷酸化水平衡量)时,AMPK活性在G1/S期到M期转换过程中的时空动态与特征明确的“染色体乘客”蛋白(如极光激酶B、染色体乘客复合体蛋白或组蛋白H3)极为相似。AMPK活性形式的有丝分裂激酶行为可能代表一种候选分子联系,通过它能量状态可直接影响肿瘤发生。明确磷酸化的AMPKα(苏氨酸172)在协调有丝分裂的染色体和细胞骨架事件中的作用,可能会彻底改变我们目前对其他与AMPK相关疾病(如肥胖、心脏肥大或加速衰老综合征)的认识。