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Regulation of CD1 Antigen-presenting Complex Stability

Odyniec, A. N. and Barral, D. C. and Garg, S. and Tatituri, R. V. and Besra, G. S. and Brenner, M. B. (2010) Regulation of CD1 Antigen-presenting Complex Stability. Journal of Biological Chemistry, 285 (16). p. 11937. ISSN 0021-9258

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URL of Published Version: http://dx.doi.org/10.1074/jbc.M109.077933

Identification Number/DOI: doi:10.1074/jbc.M109.077933

For major histocompatibility complex class I and II molecules, the binding of specific peptide antigens is essential for assembly and trafficking and is at the center of their quality control mechanism. However, the role of lipid antigen binding in stabilization and quality control of CD1 heavy chain (HC).beta(2)-microglobulin (beta(2)m) complexes is unclear. Furthermore, the distinct trafficking and loading routes of CD1 proteins take them from mildly acidic pH in early endososmal compartments (pH 6.0) to markedly acidic pH in lysosomes (pH 5.0) and back to neutral pH of the cell surface (pH 7.4). Here, we present evidence that the stability of each CD1 HC.beta(2)m complex is determined by the distinct pH optima identical to that of the intracellular compartments in which each CD1 isoform resides. Although stable at acidic endosomal pH, complexes are only stable at cell surface pH 7.4 when bound to specific lipid antigens. The proposed model outlines a quality control program that allows lipid exchange at low endosomal pH without dissociation of the CD1 HC.beta(2)m complex and then stabilizes the antigen-loaded complex at neutral pH at the cell surface.

Type of Work:Article
Date:2010 (Publication)
School/Faculty:Colleges (2008 onwards) > College of Life & Environmental Sciences
Subjects:QR Microbiology
Institution:University of Birmingham
Copyright Holders:The American Society for Biochemistry and Molecular Biology
ID Code:398
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