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Tuning an endoplasmic reticulum chaperone to the cell's needs
Author(s) -
Ron David
Publication year - 2017
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.31.1_supplement.526.5
Subject(s) - endoplasmic reticulum , unfolded protein response , chaperone (clinical) , protein folding , microbiology and biotechnology , secretory pathway , calnexin , biology , computational biology , bioinformatics , medicine , golgi apparatus , calreticulin , pathology
A transcriptional and translational program that strives to match the complement of chaperones in the endoplasmic reticulum (ER) to the burden of unfolded proteins in the early secretory pathway (the Unfolded Protein Response) has long been known to exist and its functional importance has been showcased by genetic and pharmacological manipulations. However, theoretical considerations supported by experimental observations, highlight the latency inherent in this gene expression program and suggest the potential importance of post‐translational adaptations that operate on a shorter time scale. In this talk I shall provide a very brief overview of the Unfolded Protein Response and focus the discussion on some recent observations on an ER‐localized post‐translational circuitry that tunes the activity of the compartment's resident Hsp70 protein, BiP, to rapid fluctuations in unfolded protein load. Support or Funding Information Supported by a Wellcome Trust Principal Research Fellowship to DR (2008/Z/16/Z) and Wellcome Trust Centre Grant to the CIMR (100140)