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Comment
. 2016 Sep 1;63(5):721-3.
doi: 10.1016/j.molcel.2016.08.017.

Division of Labor: ER-Resident BiP Co-Chaperones Match Substrates to Fates Based on Specific Binding Sequences

Daniel N Hebert  1 , Eugenia M Clerico  2 , Lila M Gierasch  3
Affiliations
Comment

Division of Labor: ER-Resident BiP Co-Chaperones Match Substrates to Fates Based on Specific Binding Sequences

Daniel N Hebert et al. Mol Cell. .

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.

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Figures

Figure 1
Figure 1. Experimental scheme for the cell-based peptide binding analysis for BiP and its co-chaperones
Top left panel, ER-targeted constructs were created that contain 25-amino acid long overlapping segments from two bona fide BiP substrates, mHC and NS1. Top right panel, peptide constructs were co-expressed in COS-1 cells with BiP or its co-chaperones and metabolically labelled with [35S]-Met/Cys. Bottom right panel, BiP and co-chaperone binding to the peptides was monitored by co-immunopreciptation and resolved by SDS-PAGE and autoradiography. Bottom left panel, the aggregation propensity of peptides and proteins were analyzed using the TANGO algorithm. Peptides and proteins were mutated to alter aggregation propensity and then re-analyzed for chaperone binding.
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Comment on

References

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