Keywords:
PEPTIDE
;
CELLS
;
Germany
;
IN-VIVO
;
MOLECULES
;
MICE
;
COMPLEX
;
RESPONSES
;
COMPLEXES
;
ANTIGEN
;
T-CELL
;
T-CELLS
;
MOLECULE
;
IMMUNE-RESPONSES
;
RECOGNITION
;
NUMBER
;
antigen presentation
;
PEPTIDES
;
MHC CLASS-I
;
CD8(+)
;
IMMUNE-RESPONSE
;
LOADING COMPLEX
;
ENDOPLASMIC-RETICULUM
;
SURFACE EXPRESSION
;
T-cell response
;
CROSS-PRESENTATION
;
DISULFIDE BOND FORMATION
;
review
;
RE
;
assembly
;
TRANSPORTER
;
PROTEIN-SYNTHESIS
;
endoplasmic reticulum
;
CHAPERONE
;
EXOGENOUS ANTIGENS
;
PEPTIDE-BINDING
Abstract:
Assembly of major histocompatibility complex (MHC) class I molecules in the endoplasmic reticulum is a highly coordinated process that results in abundant class I/peptide complexes at the cell surface for recognition by CD8(+) T cells and natural killer cells. During the assembly process, a number of chaperones and accessory molecules, such as transporter associated with antigen processing, tapasin, ER60, and calreticulin, assist newly synthesized class I molecules to facilitate loading of antigenic peptides and to optimize the repertoire of surface class I/peptide complexes. This review focuses on the relative importance of these accessory molecules for CD8(+) T-cell responses in vivo and discusses reasons that may help explain why some CD8(+) T-cell responses develop normally in mice deficient in components of class I assembly, despite impaired antigen presentation
Type of Publication:
Journal article published
Deep Link:
http://www.dkfz.de/cgi-bin/sel?http://www.dkfz.de/PublicationManager/Show/ShowJournal.aspx%3fpublishedId=2080
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