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Lack of tyrosine 320 impairs spontaneous endocytosis and enhances release of HLA-B27 molecules

Lack of tyrosine 320 impairs spontaneous endocytosis and enhances release of HLA-B27 molecules
Lack of tyrosine 320 impairs spontaneous endocytosis and enhances release of HLA-B27 molecules
Several lines of evidence suggest that endocytosis of MHC class I molecules requires conserved motifs within the cytoplasmic domain. In this study, we show, in the C58 rat thymoma cell line transfected with HLA-B27 molecules, that replacement of the highly conserved tyrosine (Tyr320) in the cytoplasmic domain of HLA-B27 does not hamper cell surface expression of 2-microglobulin H chain heterodimers or formation of misfolded molecules. However, Tyr320 replacement markedly impairs spontaneous endocytosis of HLA-B27. Although wild-type molecules are mostly internalized via endosomal compartments, Tyr320-mutated molecules remain at the plasma membrane in which partial colocalization with endogenous transferrin receptors can be observed, also impairing their endocytosis. Finally, we show that Tyr320 substitution enhances release of cleaved forms of HLA-B27 from the cell surface. These studies show for the first time that Tyr320 is most likely part of a cytoplasmic sorting motif involved in spontaneous endocytosis and shedding of MHC class I molecules.
0022-1767
2942-2949
Santos, Susana G.
b9bc0f2b-4cd0-4ee1-8d21-6b07f6260153
Antoniou, Antony N.
3d711a3b-f688-46f9-823e-5bb925d10ea8
Sampaio, Paula
363f2a91-d43e-4fbf-a12a-559cf021e248
Powis, Simon J.
1bdcdc68-9097-459d-9675-7bb408316bf9
Arosa, Fernando A.
77a4f30b-a78a-4906-881c-01b221f8bc9f
Santos, Susana G.
b9bc0f2b-4cd0-4ee1-8d21-6b07f6260153
Antoniou, Antony N.
3d711a3b-f688-46f9-823e-5bb925d10ea8
Sampaio, Paula
363f2a91-d43e-4fbf-a12a-559cf021e248
Powis, Simon J.
1bdcdc68-9097-459d-9675-7bb408316bf9
Arosa, Fernando A.
77a4f30b-a78a-4906-881c-01b221f8bc9f

Santos, Susana G., Antoniou, Antony N., Sampaio, Paula, Powis, Simon J. and Arosa, Fernando A. (2006) Lack of tyrosine 320 impairs spontaneous endocytosis and enhances release of HLA-B27 molecules. The Journal of Immunology, 176 (5), 2942-2949.

Record type: Article

Abstract

Several lines of evidence suggest that endocytosis of MHC class I molecules requires conserved motifs within the cytoplasmic domain. In this study, we show, in the C58 rat thymoma cell line transfected with HLA-B27 molecules, that replacement of the highly conserved tyrosine (Tyr320) in the cytoplasmic domain of HLA-B27 does not hamper cell surface expression of 2-microglobulin H chain heterodimers or formation of misfolded molecules. However, Tyr320 replacement markedly impairs spontaneous endocytosis of HLA-B27. Although wild-type molecules are mostly internalized via endosomal compartments, Tyr320-mutated molecules remain at the plasma membrane in which partial colocalization with endogenous transferrin receptors can be observed, also impairing their endocytosis. Finally, we show that Tyr320 substitution enhances release of cleaved forms of HLA-B27 from the cell surface. These studies show for the first time that Tyr320 is most likely part of a cytoplasmic sorting motif involved in spontaneous endocytosis and shedding of MHC class I molecules.

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Published date: 2006

Identifiers

Local EPrints ID: 26592
URI: http://eprints.soton.ac.uk/id/eprint/26592
ISSN: 0022-1767
PURE UUID: 243cfeaf-69a7-4e75-b794-a48e8838a838

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Date deposited: 10 Apr 2006
Last modified: 15 Jul 2019 19:13

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