A ribosome-associating factor chaperones tail-anchored membrane proteins

Malaiyalam Mariappan, Xingzhe Li, Sandra Stefanovic, Ajay Sharma, Agnieszka Mateja, Robert J. Keenan and Ramanujan S. Hegde ()
Additional contact information
Malaiyalam Mariappan: Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health
Xingzhe Li: Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health
Sandra Stefanovic: 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
Agnieszka Mateja: 929 East 57th Street, University of Chicago
Robert J. Keenan: 929 East 57th Street, University of Chicago
Ramanujan S. Hegde: Cell Biology and Metabolism Program, National Institute of Child Health and Human Development, National Institutes of Health

Nature, 2010, vol. 466, issue 7310, 1120-1124

Abstract: Bat3: a chaperone to TA proteins Tail-anchored (TA) proteins have a single transmembrane domain at their C-termini and are post-translationally targeted to the endoplasmic reticulum via the cytosolic ATPase, TRC40. In this study, Mariappan et al. identify a conserved protein complex called Bat3 complex that is recruited to ribosomes and interacts with the transmembrane domain of newly released TA proteins, transferring them to TRC40 for subsequent targeting to the endoplasmic reticulum. Thus the Bat3 complex functions as a transmembrane-domain-specific chaperone that channels TA proteins to the TRC40 insertion pathway.

Date: 2010
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/nature09296 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:466:y:2010:i:7310:d:10.1038_nature09296

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

DOI: 10.1038/nature09296

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 ().