HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain
HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain
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HDJC9 是一种新型人类 C 型 DnaJ/HSP40 成员，通过 J 结构域与 HSP70 相互作用并共伴侣。
DOI：
10.1016/j.bbrc.2006.12.013
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发表时间：
2007-02-09
影响因子：
3.1
通讯作者：
Cao, Xuetao
中科院分区：
文献类型：
--
作者：
Han, Chaofeng;Chen, Taoyong;Cao, Xuetao
hsp40是热休克蛋白（HSPs）的一个亚家族，作为hsp70的伴侣，在调节细胞增殖、存活和凋亡中发挥重要作用。迄今为止，从大肠杆菌到智人等不同物种中已鉴定出数百种HSP40蛋白。在这里，我们报道了一个新的人类C型DnaJ同源物HDJC9的克隆和特性，它包含一个典型的n端J结构域。HDJC9在各种应激和有丝分裂刺激下mRNA和蛋白水平均上调。HDJC9在正常培养条件下主要定位于细胞核，在热休克胁迫下通过非经典的脂质依赖途径转运到细胞质和质膜中。HDJC9可以与hsp70相互作用，激活hsp70的atp酶活性，两者都依赖于J结构域。我们的数据表明HDJC9是hsp70的一种新型伴侣。(c) 2006爱思唯尔公司版权所有。
HSP40s are a subfamily of heat shock proteins (HSPs) and play important roles in regulation of cell proliferation, survival and apoptosis by serving as chaperones for HSP70s. Up to date hundreds of HSP40 proteins derived from various species ranging from Escherichia coli to homo sapiens have been identified. Here we report the cloning and characterization of a novel human type C DnaJ homologue, HDJC9, containing a typical N-terminal J domain. HDJC9 is upregulated at both mRNA and protein levels upon various stress and mitogenic stimulations. HDJC9 is mainly localized in cell nuclei under normal culture conditions while it is transported into cytoplasm and plasma membrane upon heat shock stress through a non-classical and lipid-dependent pathway. HDJC9 can interact with HSP70s and activate the ATPase activity of HSP70s, both of which are dependent on the J domain. Our data suggest that HDJC9 is a novel cochaperone for HSP70s. (c) 2006 Elsevier Inc. All rights reserved.