Association of tapasin and COPI provides a mechanism for the retrograde transport of major histocompatibility complex (MHC) class I molecules from the Golgi complex to the endoplasmic reticulum

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Association of tapasin and COPI provides a mechanism for the retrograde transport of major histocompatibility complex (MHC) class I molecules from the Golgi complex to the endoplasmic reticulum. / Paulsson, Kajsa M; Kleijmeer, Monique J; Griffith, Janice; Jevon, Marc; Chen, Shangwu; Anderson, Per O; Sjögren, Hans Olov; Li, Su-Ling; Wang, Ping.

In: Journal of Biological Chemistry, Vol. 277, No. 21, 24.05.2002, p. 18266-18271.

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T1 - Association of tapasin and COPI provides a mechanism for the retrograde transport of major histocompatibility complex (MHC) class I molecules from the Golgi complex to the endoplasmic reticulum

AU - Paulsson, Kajsa M

AU - Kleijmeer, Monique J

AU - Griffith, Janice

AU - Jevon, Marc

AU - Chen, Shangwu

AU - Anderson, Per O

AU - Sjögren, Hans Olov

AU - Li, Su-Ling

AU - Wang, Ping

PY - 2002/5/24

Y1 - 2002/5/24

N2 - Tapasin is a subunit of the transporter associated with antigen processing (TAP). It associates with the major histocompatibility complex (MHC) class I. We show that tapasin interacts with beta- and gamma-subunits of COPI coatomer. COPI retrieves membrane proteins from the Golgi network back to the endoplasmic reticulum (ER). The COPI subunit-associated tapasin also interacts with MHC class I molecules suggesting that tapasin acts as the cargo receptor for packing MHC class I molecules as cargo proteins into COPI-coated vesicles. In tapasin mutant cells, neither TAP nor MHC class I are detected in association with the COPI coatomer. Interestingly, tapasin-associated MHC class I molecules are antigenic peptide-receptive and detected in both the ER and the Golgi. Our data suggest that tapasin is required for the COPI vesicle-mediated retrograde transport of immature MHC class I molecules from the Golgi network to the ER.

AB - Tapasin is a subunit of the transporter associated with antigen processing (TAP). It associates with the major histocompatibility complex (MHC) class I. We show that tapasin interacts with beta- and gamma-subunits of COPI coatomer. COPI retrieves membrane proteins from the Golgi network back to the endoplasmic reticulum (ER). The COPI subunit-associated tapasin also interacts with MHC class I molecules suggesting that tapasin acts as the cargo receptor for packing MHC class I molecules as cargo proteins into COPI-coated vesicles. In tapasin mutant cells, neither TAP nor MHC class I are detected in association with the COPI coatomer. Interestingly, tapasin-associated MHC class I molecules are antigenic peptide-receptive and detected in both the ER and the Golgi. Our data suggest that tapasin is required for the COPI vesicle-mediated retrograde transport of immature MHC class I molecules from the Golgi network to the ER.

KW - Non-U.S. Gov't

KW - Subcellular Fractions/metabolism

KW - Support

KW - Histocompatibility Antigens Class I/metabolism

KW - Immunoglobulins/metabolism

KW - Golgi Apparatus/metabolism

KW - Endoplasmic Reticulum/metabolism

KW - Coat Protein Complex I/metabolism

KW - Cell Line

KW - Antiporters/metabolism

KW - Biological Transport

U2 - 10.1074/jbc.M201388200

DO - 10.1074/jbc.M201388200

M3 - Article

C2 - 11884415

VL - 277

SP - 18266

EP - 18271

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 1083-351X

IS - 21

ER -