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Science 29 November 1985:
Vol. 230. no. 4729, pp. 1003 - 1008
DOI: 10.1126/science.2865810
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Articles

Science, Vol 230, Issue 4729, 1003-1008
Copyright © 1985 by American Association for the Advancement of Science

articles

A glycophospholipid tail at the carboxyl terminus of the Thy-1 glycoprotein of neurons and thymocytes

AG Tse, AN Barclay, A Watts, and AF Williams

Cell surface molecules of eukaryotic cells have been considered to be integrated into the membrane bilayer by a transmembrane protein sequence. The Thy-1 antigen of rodent thymocytes and brain was the first eukaryotic membrane molecule for which biochemical data clearly suggested membrane integration via a nonprotein tail. Direct evidence is now presented showing that a glycophospholipid structure is attached to the carboxyl-terminal cysteine residue and that 31 carboxyl-terminal amino acids predicted from the Thy-1 complementary DNA sequence are not present in the mature glycoprotein. These experimental results raise questions concerning signaling across a cell membrane since antibodies to Thy-1 can stimulate T lymphocytes to release lymphokines and undergo cell division.


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