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Article

Differential phosphorylation-based regulation of αB-crystallin chaperone activity for multipass transmembrane proteins.

Biochemical and biophysical research communications - 14 Oct 2016

Ciano Michela, Allocca Simona, Ciardulli Maria Camilla, Della Volpe Lucrezia, Bonatti Stefano, D'Agostino Massimo

Abstract excerpt

We have previously shown that αB-crystallin (CRYAB), a small heat shock protein (sHsp) that prevents irreversible aggregation of unfolded protein by an ATP-independent chaperone activity, plays a pivotal role in the biogenesis of multipass transmembrane proteins (TMPs) assisting their folding from the cytosolic side of the endoplasmic reticulum (ER) (D'Agostino et al., 2013). Here we present evidence, based on...

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Identifiers

PMID: 27641668
DOI: 10.1016/j.bbrc.2016.09.071
PMCID: PMC5053547

Genes

CRYAB

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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