Department of Physiology and Pharmacology and the Hotchkiss Brain Institute, University of Calgary, Calgary, AB T2N 4N1, Canada.
Biochem Cell Biol. 2010 Apr;88(2):157-65. doi: 10.1139/o09-124.
Cysteine string protein (CSPalpha, also called DnaJC5) is unique among J proteins. Similar to other J proteins, CSPalpha interacts with and activates the ATPase of Hsc70s (heat shock proteins of 70 kDa), thereby harnessing the ATPase activity for conformational work on client proteins. In contrast to other J proteins, CSPalpha is anchored to synaptic vesicles, as well as to exocrine, endocrine and neuroendocrine secretory granules, and has been shown to have an essential anti-neurodegenerative role. CSPalpha-null organisms exhibit progressive neurodegeneration, behavioural deficits, and premature death, most likely due to the progressive misfolding of one or more client proteins. Here we highlight recent advances in our understanding of the critical role that CSPalpha plays in governing exocytotic secretory functions.
半胱氨酸-string 蛋白（CSPalpha，也称为 DnaJC5）是 J 蛋白家族中的独特成员。与其他 J 蛋白相似，CSPalpha 与 Hsc70s（热休克蛋白 70kDa）的 ATP 酶相互作用并激活该酶，从而利用 ATP 酶活性对客户蛋白进行构象改变。与其他 J 蛋白不同的是，CSPalpha 锚定在突触小泡上，以及外分泌、内分泌和神经内分泌分泌颗粒上，并被证明具有重要的抗神经退行性作用。CSPalpha 缺失的生物体表现出进行性神经退行性变、行为缺陷和过早死亡，这很可能是由于一个或多个客户蛋白的渐进性错误折叠。在这里，我们强调了最近在理解 CSPalpha 在调节胞吐分泌功能方面的关键作用方面取得的进展。
