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ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function

ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_bf08851619654161a435709327ef2900

ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function

About this item

Full title

ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function

Publisher

London: Nature Publishing Group UK

Journal title

Communications biology, 2021-12, Vol.4 (1), p.1350-1350, Article 1350

Language

English

Formats

Publication information

Publisher

London: Nature Publishing Group UK

More information

Scope and Contents

Contents

Proteostasis is a challenge for cellular organisms, as all known protein synthesis machineries are error-prone. Here we show by cell fractionation and microscopy studies that misfolded proteins formed in the endoplasmic reticulum can become associated with and partly transported into mitochondria, resulting in impaired mitochondrial function. Block...

Alternative Titles

Full title

ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_doaj_primary_oai_doaj_org_article_bf08851619654161a435709327ef2900

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_bf08851619654161a435709327ef2900

Other Identifiers

ISSN

2399-3642

E-ISSN

2399-3642

DOI

10.1038/s42003-021-02873-w

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