Hsp47 promotes biogenesis of multi-subunit neuroreceptors in the endoplasmic reticulum.

ABSTRACT: Protein homeostasis (proteostasis) deficiency is an important contributing factor to neurological and metabolic diseases. However, how the proteostasis network orchestrates the folding and assembly of multi-subunit membrane proteins is poorly understood. Previous proteomics studies identified Hsp47 (Gene: SERPINH1), a heat shock protein in the endoplasmic reticulum lumen, as the most enriched interacting chaperone for gamma-aminobutyric acid type A (GABA_A) receptors. Here, we show that Hsp47 enhances the functional surface expression of GABA_A receptors in rat neurons and human HEK293T cells. Furthermore, molecular mechanism study demonstrates that Hsp47 acts after BiP (Gene: HSPA5) and preferentially binds the folded conformation of GABA_A rece

SUBMITTER: Wang YJ 

PROVIDER: S-EPMC11257679 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature