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Hulpke, S.* ; Tomioka, M.* ; Kremmer, E. ; Ueda, K.* ; Abele, R.* ; Tampé, R.*

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.

Cell. Mol. Life Sci. 69, 3317-3327 (2012)
DOI PMC
Open Access Gold möglich sobald Verlagsversion bei der ZB eingereicht worden ist.
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 TMD(0), which is correctly targeted to and inserted into the ER membrane. In the absence of coreTAP, each TMD(0) 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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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter ABC transporter; Antigen processing; Membrane protein interaction; Macromolecular membrane complex; Tapasin; Antigen-Processing Tap; Endoplasmic-Reticulum; Abc Transporter; Transmembrane Domain; Tapasin Binding; Subunit; Protein; Identification; Trafficking; HLA
ISSN (print) / ISBN 1420-682X
e-ISSN 1420-9071
Zeitschrift Cellular and Molecular Life Sciences - CMLS
Quellenangaben Band: 69, Heft: 19, Seiten: 3317-3327 Artikelnummer: , Supplement: ,
Verlag Birkhäuser
Begutachtungsstatus Peer reviewed
Institut(e) Institute of Molecular Immunology (IMI)