Characterizing the N-terminal processing motif of MHC class I ligands
| Autor: | Stefan Tenzer, Björn Peters, Sascha Bulik, Nina Ullrich, Hermann-Georg Holzhütter, Hansjörg Schild, Peter van Endert, Mark M. Schatz, Oliver Carroll, Hans-Georg Rammensee, Alejandra Nacarino Martinez, Nadja Akkad |
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| Rok vydání: | 2008 |
| Předmět: |
Proteasome Endopeptidase Complex
Immunology Amino Acid Motifs Endoplasmic Reticulum Ligands Aminopeptidase Aminopeptidases Cell Line Mice Cytosol Cell Line Tumor MHC class I Immunology and Allergy Animals Humans Amino Acid Sequence ATP Binding Cassette Transporter Subfamily B Member 2 Peptide sequence Antigen Presentation biology Ligand Endoplasmic reticulum Histocompatibility Antigens Class I Transporter associated with antigen processing Peptide Fragments N-terminus Biochemistry Proteasome biology.protein ATP-Binding Cassette Transporters Peptides HeLa Cells Protein Binding |
| Zdroj: | Journal of immunology (Baltimore, Md. : 1950). 180(5) |
| ISSN: | 0022-1767 |
| Popis: | Most peptide ligands presented by MHC class I molecules are the product of an intracellular pathway comprising protein breakdown in the cytosol, transport into the endoplasmic reticulum, and successive N-terminal trimming events. The efficiency of each of these processes depends on the amino acid sequence of the presented ligand and its precursors. Thus, relating the amino acid composition N-terminal of presented ligands to the sequence specificity of processes in the pathway gives insight into the usage of ligand precursors in vivo. Examining the amino acid composition upstream the true N terminus of MHC class I ligands, we demonstrate the existence of a distinct N-terminal processing motif comprising approximately seven residues and matching the known preferences of proteasome and TAP, two key players in ligand processing. Furthermore, we find that some residues, which are preferred by both TAP and the proteasome, are underrepresented at positions immediately preceding the N terminus of MHC class I ligands. Based on experimentally determined aminopeptidase activities, this pattern suggests trimming next to the final N terminus to take place predominantly in the endoplasmic reticulum. |
| Databáze: | OpenAIRE |
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