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Science 21 February 1986:
Vol. 231. no. 4740, pp. 823 - 829
DOI: 10.1126/science.3003913
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Articles

Science, Vol 231, Issue 4740, 823-829
Copyright © 1986 by American Association for the Advancement of Science

articles

Cell surface molecule associated with lymphocyte homing is a ubiquitinated branched-chain glycoprotein

M Siegelman, MW Bond, WM Gallatin, T St John, HT Smith, VA Fried, and IL Weissman

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 conserved polypeptide to the cell surface and leads to a proposed model of the receptor complex as a core polypeptide modified by glycosylation and ubiquitination. Independent antibodies to ubiquitin serve to identify additional cell surface species, an indication that ubiquitination of cell surface proteins may be more general. It is proposed that functional binding of lymphocytes to lymph node high endothelial venules might involve the ubiquitinated region of the receptor; if true, cell surface ubiquitin could play a more general role in cell-cell interaction and adhesion.


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