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The 170 kDa glucose regulated stress protein is a large HSP70‐ HSP110‐like protein of the endoplasmic reticulum
Author(s) -
Chen Xing,
Easton Douglas,
Oh Hyun-Ju,
Lee-Yoon Dong-Sin,
Liu Xiaoguang,
Subjeck John
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00011-7
Subject(s) - endoplasmic reticulum , hsp70 , biology , glucose regulated protein , complementary dna , glycoprotein , protein folding , microbiology and biotechnology , chaperone (clinical) , heat shock protein , biochemistry , unfolded protein response , gene , medicine , pathology
The existence of a family of unusually large and highly diverged hsp70‐like proteins (the hsp110/SSE family) has recently been described. The 170 kDa glucose regulated stress protein (grp170) is a retained endoplasmic reticulum glycoprotein that may be involved in immunoglobulin folding and/or assembly. We describe here the cloning of the cDNA for grp170 and show that it, like hsp110, is a large and highly diverged hsp70‐like polypeptide which shares specific features with hsp70 (the dnaK family) and the hsp110/SSE family, while also differing from both. Grp170 contains an ATP binding domain and binds ATP, it possesses a carboxyl terminal NDEL sequence, and its mRNA is anoxia inducible.