Daugaard Mads, Rohde Mikkel, Jäättelä Marja
Apoptosis Department and Centre for Genotoxic Stress Response, Institute of Cancer Biology, Danish Cancer Society, Strandboulevarden 49, DK-2100 Copenhagen, Denmark.
FEBS Lett. 2007 Jul 31;581(19):3702-10. doi: 10.1016/j.febslet.2007.05.039. Epub 2007 May 25.
The human heat shock protein 70 (Hsp70) family contains at least eight homologous chaperone proteins. Endoplasmatic reticulum and mitochondria have their specific Hsp70 proteins, whereas the remaining six family members reside mainly in the cytosol and nucleus. The requirement for multiple highly homologous although different Hsp70 proteins is still far from clear, but their individual and tissue-specific expression suggests that they are assigned distinct biological tasks. This concept is supported by the fact that mice knockout for different Hsp70 genes display remarkably discrete phenotypes. Moreover, emerging data suggest that individual Hsp70 proteins can bring about non-overlapping and chaperone-independent functions essential for growth and survival of cancer cells. This review summarizes our present knowledge of the individual members of human Hsp70 family and elaborate on the functional differences between the cytosolic/nuclear representatives.
人类热休克蛋白70（Hsp70）家族至少包含八种同源伴侣蛋白。内质网和线粒体有其特定的Hsp70蛋白，而其余六个家族成员主要存在于细胞质和细胞核中。虽然需要多种高度同源但不同的Hsp70蛋白，但其原因仍远未明确，不过它们各自的和组织特异性表达表明它们被赋予了不同的生物学任务。不同Hsp70基因敲除的小鼠表现出明显不同的表型，这一事实支持了这一概念。此外，新出现的数据表明，单个Hsp70蛋白可以发挥对癌细胞生长和存活至关重要的非重叠且独立于伴侣功能的作用。本综述总结了我们目前对人类Hsp70家族各个成员的认识，并阐述了细胞质/细胞核代表之间的功能差异。
