PAT in the ER for Transmembrane Protein Folding

Prabuddha S Pathinayake; Alan C-Y Hsu; Peter A B Wark

doi:10.1016/j.tibs.2020.10.001

PAT in the ER for Transmembrane Protein Folding

Trends Biochem Sci. 2020 Dec;45(12):1007-1008. doi: 10.1016/j.tibs.2020.10.001. Epub 2020 Oct 17.

Authors

Prabuddha S Pathinayake¹, Alan C-Y Hsu², Peter A B Wark³

Affiliations

¹ Priority Research Centre for Healthy Lungs, Hunter Medical Research Institute and School of Medicine and Public Health, University of Newcastle, Newcastle, NSW, Australia. Electronic address: Prabuddha.Pathinayake@newcastle.edu.au.
² Priority Research Centre for Healthy Lungs, Hunter Medical Research Institute and School of Medicine and Public Health, University of Newcastle, Newcastle, NSW, Australia.
³ Priority Research Centre for Healthy Lungs, Hunter Medical Research Institute and School of Medicine and Public Health, University of Newcastle, Newcastle, NSW, Australia; Department of Respiratory and Sleep Medicine, John Hunter Hospital, Newcastle, NSW, Australia.

PMID: 33082068
DOI: 10.1016/j.tibs.2020.10.001

Abstract

Integral membrane proteins (IMPs) have crucial roles in many cellular processes. A novel intramembrane chaperone complex, recently elucidated by Chitwood and Hedge, provides mechanistic insight of IMP biogenesis and folding, illustrating how IMPs with multiple transmembrane domains (TMDs) are assembled within the endoplasmic reticulum (ER) membrane.

Keywords: PAT complex; chaperone; endoplasmic reticulum; membrane proteins.

Publication types

Comment

MeSH terms

Endoplasmic Reticulum* / metabolism
Membrane Proteins* / metabolism
Protein Biosynthesis
Protein Domains
Protein Folding

Substances

Membrane Proteins