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Structural analysis of class I MHC molecules: The cytoplasmic domain is not required for cytoskeletal association, aggregation and internalization

  • Hanan Gur*
  • , Thomas D. Geppert
  • , Peter E. Lipsky
  • *Corresponding author for this work
  • University of Texas Southwestern Medical Center
  • Sheba Medical Center at Tel Hashomer

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

The role of the cytoplasmic domain in a variety of the functional activities of class I MHC molecules has not been documented. To address this question, Jurkat cells were transfected with genes for either native class I MHC molecules or constructs in which all but four cytoplasmic amino acids were deleted. Antibody-induced aggregation and internalization of class I MHC molecules were examined by flow cytometry, and cytoskeletal association was determined by analyzing the detergent-resistant fraction of FITC- labeled mAb to class I molecules. The results indicate that the truncated class I MHC molecules are comparable to native class I MHC molecules in the ability to move in the plane of the membrane and aggregate, to associate with the cytoskeleton and to undergo mAb-induced internalization at 37 C. Thus, the cyloplasmic domain of class I MHC molecules is not required for these functional activities.

Original languageEnglish
Pages (from-to)125-132
Number of pages8
JournalMolecular Immunology
Volume34
Issue number2
DOIs
StatePublished - Feb 1997
Externally publishedYes

Funding

FundersFunder number
National Institutes of HealthAR-39169
National Institute of Arthritis and Musculoskeletal and Skin DiseasesP01AR009989

    Keywords

    • Class I MHC molecules
    • aggregation
    • cytoskeleton
    • internalization

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