Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada M5S 1A8.
FEBS Lett. 2013 Apr 17;587(8):1067-72. doi: 10.1016/j.febslet.2013.02.018. Epub 2013 Feb 19.
Molecular chaperones are an essential group of proteins required to maintain proper protein homeostasis in the cell and include Hsp40, Hsp60, Hsp70, Hsp90, and Hsp100 among others. Hsp110 proteins form a subfamily of the Hsp70 family and seem to primarily function as nucleotide exchange factors for the Hsp70s. Data to date suggest that Hsp110 together with Hsp70 are required to ensure proper spindle assembly and nuclear distribution during cell division. More specifically, we propose that an Hsp110-Hsp70 complex modulates the activity and directionality of the kinesin-5 motor, Cin8, which is required for spindle elongation. The modulation of spindle length by molecular chaperones might be a mechanism by which cell division can be controlled especially under proteostatic stress.
分子伴侣是一组必需的蛋白质，对于维持细胞内蛋白质的正常状态至关重要，包括 Hsp40、Hsp60、Hsp70、Hsp90 和 Hsp100 等。Hsp110 蛋白是 Hsp70 家族的一个亚家族，似乎主要作为 Hsp70 的核苷酸交换因子发挥作用。迄今为止的数据表明，Hsp110 与 Hsp70 一起确保细胞分裂过程中纺锤体的正确组装和核分布。更具体地说，我们提出 Hsp110-Hsp70 复合物调节驱动蛋白-5 电机 Cin8 的活性和方向性，这对于纺锤体伸长是必需的。分子伴侣对纺锤体长度的调节可能是细胞分裂可以被控制的一种机制，特别是在蛋白质稳态应激下。
