PAT in the ER for Transmembrane Protein Folding

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

Comment

PAT in the ER for Transmembrane Protein Folding

Prabuddha S Pathinayake et al. Trends Biochem Sci. 2020 Dec.

. 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

Erratum in

PAT in the ER for Transmembrane Protein Folding: (Trends in Biochemical Sciences 45 (2020) 1007-1008).
Pathinayake PS, Hsu AC, Wark PAB. Pathinayake PS, et al. Trends Biochem Sci. 2021 Apr;46(4):344. doi: 10.1016/j.tibs.2020.12.001. Epub 2021 Jan 5. Trends Biochem Sci. 2021. PMID: 33413995 No abstract available.

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.

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Comment on

An intramembrane chaperone complex facilitates membrane protein biogenesis.
Chitwood PJ, Hegde RS. Chitwood PJ, et al. Nature. 2020 Aug;584(7822):630-634. doi: 10.1038/s41586-020-2624-y. Epub 2020 Aug 19. Nature. 2020. PMID: 32814900 Free PMC article.

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PAT in the ER for Transmembrane Protein Folding

Affiliations

PAT in the ER for Transmembrane Protein Folding

Authors

Affiliations

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