Peptide length and sequence specificity of the mouse TAP1/TAP2 translocator

Ton N M Schumacher, Devang V. Kantesaria, Marie Therese Heemels, Philip G. Ashton-Rickardt, James C. Shepherd, Klaus Frueh, Young Yang, Per A. Peterson, Susumu Tonegawa, Hidde L. Ploegh

Research output: Contribution to journalArticle

174 Citations (Scopus)

Abstract

The transporter associated with antigen processing (TAP) delivers peptides to the lumen of the endoplasmic reticulum in an adenosine triphosphate (ATP) dependent fashion for presentation by major histocompatibility complex class I molecules. We show that the mouse TAP translocator (H-2b haplotype) selects peptides based on a minimal size of nine residues, and on the presence of a hydrophobic COOH-terminal amino acid. The preponderance of COOH-terminal hydrophobic amino acids in peptides capable of binding to mouse class I molecules thus fits remarkably well with the specificity of the TAP translocator. In addition to transport in the lumenal direction, efflux of peptide in the cytosolic direction is observed in an ATP- and temperature- dependent manner. By maintaining a low peptide concentration at the site of class I assembly, this efflux mechanism may ensure that class I molecules are loaded preferentially with high affinity peptides.

Original languageEnglish (US)
Pages (from-to)533-540
Number of pages8
JournalJournal of Experimental Medicine
Volume179
Issue number2
StatePublished - Feb 1 1994
Externally publishedYes

Fingerprint

Peptides
trypsinogen activation peptide
Adenosine Triphosphate
Amino Acids
Major Histocompatibility Complex
Endoplasmic Reticulum
Haplotypes
Temperature
Direction compound

ASJC Scopus subject areas

  • Immunology

Cite this

Schumacher, T. N. M., Kantesaria, D. V., Heemels, M. T., Ashton-Rickardt, P. G., Shepherd, J. C., Frueh, K., ... Ploegh, H. L. (1994). Peptide length and sequence specificity of the mouse TAP1/TAP2 translocator. Journal of Experimental Medicine, 179(2), 533-540.

Peptide length and sequence specificity of the mouse TAP1/TAP2 translocator. / Schumacher, Ton N M; Kantesaria, Devang V.; Heemels, Marie Therese; Ashton-Rickardt, Philip G.; Shepherd, James C.; Frueh, Klaus; Yang, Young; Peterson, Per A.; Tonegawa, Susumu; Ploegh, Hidde L.

In: Journal of Experimental Medicine, Vol. 179, No. 2, 01.02.1994, p. 533-540.

Research output: Contribution to journalArticle

Schumacher, TNM, Kantesaria, DV, Heemels, MT, Ashton-Rickardt, PG, Shepherd, JC, Frueh, K, Yang, Y, Peterson, PA, Tonegawa, S & Ploegh, HL 1994, 'Peptide length and sequence specificity of the mouse TAP1/TAP2 translocator', Journal of Experimental Medicine, vol. 179, no. 2, pp. 533-540.
Schumacher TNM, Kantesaria DV, Heemels MT, Ashton-Rickardt PG, Shepherd JC, Frueh K et al. Peptide length and sequence specificity of the mouse TAP1/TAP2 translocator. Journal of Experimental Medicine. 1994 Feb 1;179(2):533-540.
Schumacher, Ton N M ; Kantesaria, Devang V. ; Heemels, Marie Therese ; Ashton-Rickardt, Philip G. ; Shepherd, James C. ; Frueh, Klaus ; Yang, Young ; Peterson, Per A. ; Tonegawa, Susumu ; Ploegh, Hidde L. / Peptide length and sequence specificity of the mouse TAP1/TAP2 translocator. In: Journal of Experimental Medicine. 1994 ; Vol. 179, No. 2. pp. 533-540.
@article{dc75568dc32c4bed904d9cd02edb2e96,
title = "Peptide length and sequence specificity of the mouse TAP1/TAP2 translocator",
abstract = "The transporter associated with antigen processing (TAP) delivers peptides to the lumen of the endoplasmic reticulum in an adenosine triphosphate (ATP) dependent fashion for presentation by major histocompatibility complex class I molecules. We show that the mouse TAP translocator (H-2b haplotype) selects peptides based on a minimal size of nine residues, and on the presence of a hydrophobic COOH-terminal amino acid. The preponderance of COOH-terminal hydrophobic amino acids in peptides capable of binding to mouse class I molecules thus fits remarkably well with the specificity of the TAP translocator. In addition to transport in the lumenal direction, efflux of peptide in the cytosolic direction is observed in an ATP- and temperature- dependent manner. By maintaining a low peptide concentration at the site of class I assembly, this efflux mechanism may ensure that class I molecules are loaded preferentially with high affinity peptides.",
author = "Schumacher, {Ton N M} and Kantesaria, {Devang V.} and Heemels, {Marie Therese} and Ashton-Rickardt, {Philip G.} and Shepherd, {James C.} and Klaus Frueh and Young Yang and Peterson, {Per A.} and Susumu Tonegawa and Ploegh, {Hidde L.}",
year = "1994",
month = "2",
day = "1",
language = "English (US)",
volume = "179",
pages = "533--540",
journal = "Journal of Experimental Medicine",
issn = "0022-1007",
publisher = "Rockefeller University Press",
number = "2",

}

TY - JOUR

T1 - Peptide length and sequence specificity of the mouse TAP1/TAP2 translocator

AU - Schumacher, Ton N M

AU - Kantesaria, Devang V.

AU - Heemels, Marie Therese

AU - Ashton-Rickardt, Philip G.

AU - Shepherd, James C.

AU - Frueh, Klaus

AU - Yang, Young

AU - Peterson, Per A.

AU - Tonegawa, Susumu

AU - Ploegh, Hidde L.

PY - 1994/2/1

Y1 - 1994/2/1

N2 - The transporter associated with antigen processing (TAP) delivers peptides to the lumen of the endoplasmic reticulum in an adenosine triphosphate (ATP) dependent fashion for presentation by major histocompatibility complex class I molecules. We show that the mouse TAP translocator (H-2b haplotype) selects peptides based on a minimal size of nine residues, and on the presence of a hydrophobic COOH-terminal amino acid. The preponderance of COOH-terminal hydrophobic amino acids in peptides capable of binding to mouse class I molecules thus fits remarkably well with the specificity of the TAP translocator. In addition to transport in the lumenal direction, efflux of peptide in the cytosolic direction is observed in an ATP- and temperature- dependent manner. By maintaining a low peptide concentration at the site of class I assembly, this efflux mechanism may ensure that class I molecules are loaded preferentially with high affinity peptides.

AB - The transporter associated with antigen processing (TAP) delivers peptides to the lumen of the endoplasmic reticulum in an adenosine triphosphate (ATP) dependent fashion for presentation by major histocompatibility complex class I molecules. We show that the mouse TAP translocator (H-2b haplotype) selects peptides based on a minimal size of nine residues, and on the presence of a hydrophobic COOH-terminal amino acid. The preponderance of COOH-terminal hydrophobic amino acids in peptides capable of binding to mouse class I molecules thus fits remarkably well with the specificity of the TAP translocator. In addition to transport in the lumenal direction, efflux of peptide in the cytosolic direction is observed in an ATP- and temperature- dependent manner. By maintaining a low peptide concentration at the site of class I assembly, this efflux mechanism may ensure that class I molecules are loaded preferentially with high affinity peptides.

UR - http://www.scopus.com/inward/record.url?scp=0028098173&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028098173&partnerID=8YFLogxK

M3 - Article

C2 - 8294864

AN - SCOPUS:0028098173

VL - 179

SP - 533

EP - 540

JO - Journal of Experimental Medicine

JF - Journal of Experimental Medicine

SN - 0022-1007

IS - 2

ER -