Protein targeting and degradation are coupled for elimination of mislocalized proteins

Tara Hessa, Ajay Sharma, Malaiyalam Mariappan, Heather D. Eshleman, Erik Gutierrez and Ramanujan S. Hegde ()
Additional contact information
Tara Hessa: Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health
Ajay Sharma: Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health
Malaiyalam Mariappan: Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health
Heather D. Eshleman: Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health
Erik Gutierrez: Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health
Ramanujan S. Hegde: Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health

Nature, 2011, vol. 475, issue 7356, 394-397

Abstract: Removal of 'spare' proteins Membrane proteins that fail to be delivered to the endoplasmic reticulum must be rapidly degraded to avoid inappropriate aggregation and disruption of protein homeostasis. The mechanism of this process of mislocalized protein (MLP) degradation is unknown. Here Bag6, a chaperone complex involved in protein targeting, is identified as part of this mechanism. Bag6 interacts with and captures MLPs, coupling them to the ubiquitin-mediated degradation pathway. This could potentially achieve rapid degradation of MLPs without futile engagement of the cytosolic folding machinery.

Date: 2011
References: Add references at CitEc
Citations: View citations in EconPapers (3)

Downloads: (external link)
https://www.nature.com/articles/nature10181 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:475:y:2011:i:7356:d:10.1038_nature10181

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature10181

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().