Journal article
Tetraspan cargo adaptors usher GPI-anchored proteins into multivesicular bodies
Cell cycle (Georgetown, Tex.), Vol.14(23), pp.3673-3678
12/02/2015
DOI: 10.1080/15384101.2015.1100773
PMCID: PMC4825753
PMID: 26505929
Abstract
Ubiquitinated membrane proteins are sorted into intralumenal endosomal vesicles on their way for degradation in lysosomes. Here we summarize the discovery of the Cos proteins, which work to organize and segregate ubiquitinated cargo prior to its incorporation into intralumenal vesicles of the multivesicular body (MVB). Importantly, cargoes such as GPI-anchored proteins (GPI-APs) that cannot undergo ubiquitination, rely entirely on Cos proteins for sorting into intralumenal vesicles using the same pathway that depends on ESCRTs and ubiquitin ligases that typical polytopic membrane proteins do. Here we show Cos proteins provide functions as not only adaptor proteins for ubiquitin ligases, but also as cargo carriers that can physically usher a variety of other proteins into the MVB pathway. We then discuss the significance of this new sorting model and the broader implications for this cargo adaptor mechanism, whereby yeast Cos proteins, and their likely animal analogs, provide a ubiquitin sorting signal in trans to enable sorting of a membrane protein network into intralumenal vesicles.
Details
- Title: Subtitle
- Tetraspan cargo adaptors usher GPI-anchored proteins into multivesicular bodies
- Creators
- Chris MacDonald - Molecular Physiology and Biophysics; University of IowaMark A Stamnes - Molecular Physiology and Biophysics; University of IowaDavid J Katzmann - Biochemistry and Molecular Biology; Mayo Clinic College of MedicineRobert C Piper - Molecular Physiology and Biophysics; University of Iowa
- Resource Type
- Journal article
- Publication Details
- Cell cycle (Georgetown, Tex.), Vol.14(23), pp.3673-3678
- Publisher
- Taylor & Francis
- DOI
- 10.1080/15384101.2015.1100773
- PMID
- 26505929
- PMCID
- PMC4825753
- ISSN
- 1538-4101
- eISSN
- 1551-4005
- Language
- English
- Date published
- 12/02/2015
- Academic Unit
- Molecular Physiology and Biophysics; Medicine Administration; Internal Medicine
- Record Identifier
- 9984025362802771
Metrics
23 Record Views