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Structural Characterization of a Murine Lymphocyte Homing Receptor Suggests a Ubiquitinated Branched-Chain Glycoprotein

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Proteins

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Summary

Partial amino acid sequence analysis of a purified lymphocyte homing receptor demonstrates the presence of two amino-termini, one of which corresponds precisely to the amino-terminus of ubiquitin. This observation extends the province of this extraordinarily conserved polypeptide to the cell surface, and leads to a proposed model of the receptor complex as a ubiquitinated branched-chain glycoprotein. Functional binding of lymphocytes to high endothelial venules (HEV) requires the accessibility of the ubiquitinated region of the receptor, suggesting a possible central role for ubiquitin in cell-cell interaction and adhesion.

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Author information

Authors and Affiliations

  1. Laboratory of Experimental Oncology, Department of Pathology, Stanford University School of Medicine, Stanford, CA, 94305, USA

    Mark Siegelman & Irving L. Weissman

  2. DNAX Research Institute, 901 California Avenue, Palo Alto, CA, 94306, USA

    Martha Bond

Authors
  1. Mark Siegelman
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  2. Martha Bond
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  3. Irving L. Weissman
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Editor information

Editors and Affiliations

  1. Molecular Genetics, Inc, Minnetonka, Minnesota, USA

    James J. L’Italien

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© 1987 Plenum Press, New York

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Siegelman, M., Bond, M., Weissman, I.L. (1987). Structural Characterization of a Murine Lymphocyte Homing Receptor Suggests a Ubiquitinated Branched-Chain Glycoprotein. In: L’Italien, J.J. (eds) Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1787-6_73

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  • DOI: https://doi.org/10.1007/978-1-4613-1787-6_73

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4612-9001-8

  • Online ISBN: 978-1-4613-1787-6

  • eBook Packages: Springer Book Archive

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