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Blood, 1 May 2002, Vol. 99, No. 9, pp. 3250-3255
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Constitutive and functional association of the platelet collagen
receptor glycoprotein VI-Fc receptor -chain complex with
membrane rafts
Yasuharu Ezumi,
Kumi Kodama,
Takashi Uchiyama, and
Hiroshi Takayama
From the Department of Hematology and Oncology,
Clinical Sciences for Pathological Organs, Graduate School of Medicine,
Kyoto University, Japan.
The platelet collagen receptor glycoprotein (GP) VI-Fc receptor
-chain (FcR ) complex transduces signals in an immunoreceptorlike manner. We examined a role for the Triton X-100-insoluble membrane rafts in GPVI-FcR complex signaling. Methyl- -cyclodextrin
(M CD)-induced disruption of the membrane rafts inhibited not
only platelet aggregation and secretion but also tyrosine
phosphorylation of signaling molecules on stimulation through the
GPVI-FcR complex. The GPVI-FcR complex was constitutively
associated with membrane rafts wherein the Src family kinases and LAT
were also present. Their association was not affected by the complex
engagement but was highly sensitive to M CD treatment. Thus, we
provide the first evidence that the GPVI-FcR complex is
constitutively and functionally associated with membrane rafts.

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