Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 69, Issue 19, Pages 3317-3327Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-012-1005-6
Keywords
ABC transporter; Antigen processing; Membrane protein interaction; Macromolecular membrane complex; Tapasin
Categories
Funding
- European Commission Seventh Framework Program
- Japan Society for the Promotion of Science (JSPS) [20228001]
- Grants-in-Aid for Scientific Research [20228001] Funding Source: KAKEN
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The loading of antigenic peptides onto major histocompatibility complex class I (MHC I) molecules is an essential step in the adaptive immune response against virally or malignantly transformed cells. The ER-resident peptide-loading complex (PLC) consists of the transporter associated with antigen processing (TAP1 and TAP2), assembled with the auxiliary factors tapasin and MHC I. Here, we demonstrated that the N-terminal extension of each TAP subunit represents an autonomous domain, named TMD0, which is correctly targeted to and inserted into the ER membrane. In the absence of coreTAP, each TMD0 recruits tapasin in a 1:1 stoichiometry. Although the TMD(0)s lack known ER retention/retrieval signals, they are localized to the ER membrane even in tapasin-deficient cells. We conclude that the TMD(0)s of TAP form autonomous interaction hubs linking antigen translocation into the ER with peptide loading onto MHC I, hence ensuring a major function in the integrity of the antigen-processing machinery.
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