Journal
JOURNAL OF IMMUNOLOGY
Volume 168, Issue 4, Pages 1538-1541Publisher
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.168.4.1538
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Funding
- NIAID NIH HHS [AI 14584] Funding Source: Medline
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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.
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