title: Division of Labor: ER-Resident BiP Co-Chaperones Match Substrates to Fates Based on Specific Binding Sequences.
abstract: In this issue of Molecular Cell, Behnke et al. (2016) describe a novel cell-based peptide-binding assay and use it to analyze the binding specificities of the endoplasmic reticulum Hsp70 chaperone and its co-chaperones and to probe their different roles in protein quality control.
authors: Department of Biochemistry and Molecular Biology, Life Sciences Laboratories, University of Massachusetts Amherst, 240 Thatcher Way, Amherst, MA 01003, USA; Program in Molecular and Cellular Biology, Life Sciences Laboratories, University of Massachusetts Amherst, 240 Thatcher Way, Amherst, MA 01003, USA. Electronic address: dhebert@biochem.umass.edu.
authors: Daniel N
authors: DN
authors: Hebert
authors: Department of Biochemistry and Molecular Biology, Life Sciences Laboratories, University of Massachusetts Amherst, 240 Thatcher Way, Amherst, MA 01003, USA.
authors: Eugenia M
authors: EM
authors: Clerico
authors: Department of Biochemistry and Molecular Biology, Life Sciences Laboratories, University of Massachusetts Amherst, 240 Thatcher Way, Amherst, MA 01003, USA; Program in Molecular and Cellular Biology, Life Sciences Laboratories, University of Massachusetts Amherst, 240 Thatcher Way, Amherst, MA 01003, USA; Department of Chemistry, Life Sciences Laboratories, University of Massachusetts Amherst, 240 Thatcher Way, Amherst, MA 01003, USA. Electronic address: gierasch@biochem.umass.edu.
authors: Lila M
authors: LM
authors: Gierasch
mesh_terms: D000818:Animals; D004721:Endoplasmic Reticulum / Q000737:chemistry; D018840:HSP70 Heat-Shock Proteins / Q000032:analysis; D006360:Heat-Shock Proteins / Q000032:analysis*; D006801:Humans; D018832:Molecular Chaperones / Q000032:analysis*
chemical_list: D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones