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Co‐ and Post‐Translational Protein Folding in the ER
Author(s) -
Ellgaard Lars,
McCaul Nicholas,
Chatsisvili Anna,
Braakman Ineke
Publication year - 2016
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12392
Subject(s) - endoplasmic reticulum , protein folding , biology , microbiology and biotechnology , organelle , chaperone (clinical) , folding (dsp implementation) , membrane protein , unfolded protein response , co chaperone , secretory pathway , biophysics , membrane , biochemistry , golgi apparatus , hsp90 , medicine , heat shock protein , engineering , pathology , gene , electrical engineering
The endoplasmic reticulum ( ER ) produces a plethora of membrane and secretory proteins, which must fold and assemble correctly before ER exit – if these processes fail, misfolded species accumulate in the ER or are degraded. Here, we review chaperone‐assisted co‐ and post‐translational folding and assembly in the ER and the influence of protein modifications, emphasizing how method development has advanced the field by allowing folding studies inside living cells. The laboratory of Dr Ari Helenius pioneered many of these studies with the influenza virus hemagglutinin ( HA ) protein, which is a trimer. This cartoon of an HA monomer drawn by Dr Ari Helenius shows the receptor domain (R), the esterase‐like domain (E′) and the stem domain (S). Native HA has six disulfide bonds (orange lines). A, B, E, F1 and F2 indicate the positions of antigenic epitopes.