Phosphatidylinositol is the membrane-anchoring domain of the Thy-1 glycoprotein

Glycoproteins exposed on cell surfaces are commonly anchored in the membrane via hydrophobic peptide domains which penetrate the lipid bilayer 1 . However, it has recently been appreciated that there are exceptions to this generalization and certain cell-surface proteins appear to be anchored via a...

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Bibliographic Details
Published in:Nature (London) 1985-11, Vol.318 (6041), p.62-64
Main Authors: Low, Martin G, Kincade, Paul W
Format: Article
Language:English
Subjects:
Animals
Antigens, Surface
Biological and medical sciences
Cell Membrane - ultrastructure
cell membranes
Cell membranes. Ionic channels. Membrane pores
Cell structures and functions
Fundamental and applied biological sciences. Psychology
Glycoproteins - metabolism
Humanities and Social Sciences
letter
lymphocytes T
Membrane Proteins - metabolism
Mice
Molecular and cellular biology
multidisciplinary
phosphatidylinositol
Phosphatidylinositols - metabolism
phospholipase C
Receptors, Cell Surface - metabolism
Receptors, Transferrin
Science
Science (multidisciplinary)
T-Lymphocytes - ultrastructure
Thy-1 antigen
Thy-1 Antigens
Type C Phospholipases
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Summary:Glycoproteins exposed on cell surfaces are commonly anchored in the membrane via hydrophobic peptide domains which penetrate the lipid bilayer 1 . However, it has recently been appreciated that there are exceptions to this generalization and certain cell-surface proteins appear to be anchored via a specific association with phosphatidylinositol 2–7 . Thy-1 glycoprotein may also be attached to cell membranes by a non-protein hydrophobic domain located at the C-terminus and although the chemical nature of this moiety has not been determined, it was postulated that it might be a lipid 8 . On the other hand, ammo-acid sequences predicted from nucleotide sequence analyses suggest that a C-terminal hydrophobic peptide segment not found in the purified, detergent-solubilized Thy-1 glycoprotein may be responsible for attachment 9–11 . We report here that a highly purified phospholipase C specific for phosphatidylinositol selectively released Thy-1 from viable normal or malignant T lymphocytes. This result supports the proposed lipid nature of the Thy-1 anchoring domain 8 and further suggests that this lipid is, or is closely related to, phosphatidylinositol.
ISSN:0028-0836
1476-4687
DOI:10.1038/318062a0