Novel functions of the ER-located Hsp40s DNAJB12 and DNAJB14 on proteins at the outer mitochondrial membrane under stress mediated by CCCP-Reference-Cited by-同舟云学术

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Novel functions of the ER-located Hsp40s DNAJB12 and DNAJB14 on proteins at the outer mitochondrial membrane under stress mediated by CCCP

Published:2023-10-18 Issue: Volume: Page:
ISSN:0300-8177
Container-title:Molecular and Cellular Biochemistry
language:en
Short-container-title:Mol Cell Biochem

Author:

Sopha Pattarawut,Meerod Tirawit,Chantrathonkul Bunkuea,Phutubtim Nadgrita,Cyr Douglas M.,Govitrapong Piyarat

Funder

Chulabhorn Graduate Institute, Chulabhorn Royal Academy

Thailand Research Fund

Thailand Science Research and Innovation

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Clinical Biochemistry,Molecular Biology,General Medicine

Link

https://link.springer.com/content/pdf/10.1007/s11010-023-04866-1.pdf

Reference36 articles.

1. Araki K, Nagata K (2011) Protein folding and quality control in the ER. Cold Spring Harb Perspect Biol 3:a007526. https://doi.org/10.1101/cshperspect.a007526

2. Hetz C, Zhang K, Kaufman RJ (2020) Mechanisms, regulation and functions of the unfolded protein response. Nat Rev Mol Cell Biol 21:421–438. https://doi.org/10.1038/s41580-020-0250-z

3. Ninagawa S, George G, Mori K (2021) Mechanisms of productive folding and endoplasmic reticulum-associated degradation of glycoproteins and non-glycoproteins. Biochim Biophys Acta Gen Subj 1865:129812. https://doi.org/10.1016/j.bbagen.2020.129812

4. Houck SA, Cyr DM (2012) Mechanisms for quality control of misfolded transmembrane proteins. Biochim Biophys Acta 1818:1108–1114. https://doi.org/10.1016/j.bbamem.2011.11.007

5. Phillips MJ, Voeltz GK (2016) Structure and function of ER membrane contact sites with other organelles. Nat Rev Mol Cell Biol 17:69–82. https://doi.org/10.1038/nrm.2015.8

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