PAT in the ER for Transmembrane Protein Folding.

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

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

Afiliação

Pathinayake PS; 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.
Hsu AC; Priority Research Centre for Healthy Lungs, Hunter Medical Research Institute and School of Medicine and Public Health, University of Newcastle, Newcastle, NSW, Australia.
Wark PAB; 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.

Trends Biochem Sci ; 45(12): 1007-1008, 2020 12.

Article em En | MEDLINE | ID: mdl-33082068

RESUMO

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.

Assuntos

Retículo Endoplasmático; Proteínas de Membrana; Retículo Endoplasmático/metabolismo; Proteínas de Membrana/metabolismo; Biossíntese de Proteínas; Domínios Proteicos; Dobramento de Proteína

Palavras-chave

PAT complex; chaperone; endoplasmic reticulum; membrane proteins

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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Retículo Endoplasmático / Proteínas de Membrana Idioma: En Ano de publicação: 2020 Tipo de documento: Article

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