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Vol. 10, Issue 4, 891-905, April 1999
*Department of Pathology, Centre Médical Universitaire,
CH-1211 Geneva 4, Switzerland; and §Institut für
Organische Chemie und Biochemie der Universität Bonn, D-53121
Bonn, Germany
Src family protein-tyrosine kinases are implicated in
signaling via glycosylphosphatidylinositol (GPI)-anchored
receptors. Both kinds of molecules reside in opposite leaflets of the
same sphingolipid-enriched microdomains in the lymphocyte plasma
membrane without making direct contact. Under detergent-free
conditions, we isolated a GPI-enriched plasma membrane fraction, also
containing transmembrane proteins, selectively associated with
sphingolipid microdomains. Nonionic detergents released the
transmembrane proteins, yielding core sphingolipid microdomains,
limited amounts of which could also be obtained by detergent-free
subcellular fractionation. Protein-tyrosine kinase activity in
membranes containing both GPI-anchored and transmembrane proteins was
much lower than in core sphingolipid microdomains but was strongly
reactivated by nonionic detergents. The inhibitory mechanism acting on
Lck and Fyn kinases in these membranes was independent of the
protein-tyrosine phosphatase CD45 and was characterized as a mixed,
noncompetitive one. We propose that in lymphocyte plasma membranes, Lck
and Fyn kinases exhibit optimal activity when juxtaposed to the GPI-
and sphingolipid-enriched core microdomains but encounter inhibitory conditions in surrounding membrane areas that are rich in
glycerophospholipids and contain additional transmembrane proteins.
Department of Experimental
Therapeutics, Ontario Cancer Institute, Princess Margaret Hospital, 610 University Avenue, Toronto, Ontario M5G 2M9, Canada;
Department of Biochemistry and Cell Biology, State
University of New York at Stony Brook, Stony Brook, NY 11794-5215.
Corresponding author. E-mail address:
Daniel.Hoessli{at}medecine.unige.ch.
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