Logo image
Back
Cutting edge: Tapasin is retained in the endoplasmic reticulum by dynamic clustering and exclusion from endoplasmic reticulum exit sites
Journal article   Open access   Peer reviewed

Cutting edge: Tapasin is retained in the endoplasmic reticulum by dynamic clustering and exclusion from endoplasmic reticulum exit sites

Tsvetelina Pentcheva, Elias T Spiliotis and Michael Edidin
The Journal of immunology (1950), v 168(4), pp 1538-1541
15 Feb 2002
DOI: https://doi.org/10.4049/jimmunol.168.4.1538
PMID: 11823478
Featured in Collection :   UN Sustainable Development Goals @ Drexel
url
https://doi.org/10.4049/jimmunol.168.4.1538View
Published, Version of Record (VoR)Maybe Open Access (Publisher Bronze),  Open

Abstract

Abridged Index Medicus
Tapasin retains empty or suboptimally loaded MHC class I molecules in the endoplasmic reticulum (ER). However, the molecular mechanism of this process and how tapasin itself is retained in the ER are unknown. These questions were addressed by tagging tapasin with the cyan fluorescent protein or yellow fluorescent protein (YFP) and probing the distribution and mobility of the tagged proteins. YFP-tapasin molecules were functional and could be isolated in association with TAP, as reported for native tapasin. YFP-tapasin was excluded from ER exit sites even after accumulation of secretory cargo due to disrupted anterograde traffic. Almost all tapasin molecules were clustered, and these clusters diffused freely in the ER. Tapasin oligomers appear to be retained by the failure of the export machinery to recognize them as cargo.

Metrics

11 Record Views
24 citations in Web of Science
27 citations in Scopus

Details

UN Sustainable Development Goals (SDGs)

This publication has contributed to the advancement of the following goals:

#3 Good Health and Well-Being

InCites Highlights

Data related to this publication, from InCites Benchmarking & Analytics tool:

Web of Science research areas
Immunology
Logo image