TY  - JOUR
A1  - Hulpke, Sabine
A1  - Tomioka, Maiko
A1  - Kremmer, Elisabeth
A1  - Ueda, Kazumitsu
A1  - Abele, Rupert
A1  - Tampé, Robert
T1  - Direct evidence that the N-terminal extensions of the TAP complex act as autonomous interaction scaffolds for the assembly of the MHC I peptide-loading complex
T2  - Cellular and molecular life sciences : (CMLS)
N2  - 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 TMD0s lack known ER retention/retrieval signals, they are localized to the ER membrane even in tapasin-deficient cells. We conclude that the TMD0s 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.
Y1  - 2012
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/28873
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-288735
SN  - 1420-9071
SN  - 1420-682X
N1  - Open Access This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
VL  - 69
SP  - 3317
EP  - 3327
PB  - Springer
CY  - Basel
ER  -