title: A first line of defense against ER stress.
abstract: BiP is the predominant DnaK/Hsp70-type chaperone protein in the ER. It is required for folding and assembling newly synthesized ER client proteins, yet having too much BiP inhibits folding. In this issue, Chambers et al. (2012. J. Cell Biol. doi:10.1083/jcb.201202005) report that ADP ribosylation of BiP provides a reversible switch that fine tunes BiP activity according to need.
authors.affiliation: Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, CA 94158, USA.
authors.forename: David
authors.initials: D
authors.lastname: Pincus
authors.forename: Peter
authors.initials: P
authors.lastname: Walter
mesh_terms: D000244:Adenosine Diphosphate / Q000737:chemistry*; D000818:Animals; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins / Q000502:physiology*; D006801:Humans; D011506:Proteins / Q000737:chemistry*
chemical_list: D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins; D011506:Proteins; D000244:Adenosine Diphosphate