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Vol. 12, Issue 10, 3031-3045, October 2001
Department of Biology, University of Konstanz, 78467 Konstanz,
Germany
Using confocal laser scanning and double immunogold electron
microscopy, we demonstrate that reggie-1 and -2 are colocalized in
0.1-µm plasma membrane microdomains of neurons and astrocytes. In
astrocytes, reggie-1 and -2 do not occur in caveolae but clearly outside these structures. Microscopy and coimmunoprecipitation show
that reggie-1 and -2 are associated with fyn kinase and with the
glycosylphosphatidyl inositol-anchored proteins Thy-1 and F3
that, when activated by antibody cross-linking, selectively copatch
with reggie. Jurkat cells, after cross-linking of Thy-1 or GM1 (with
the use of cholera toxin), exhibit substantial colocalization of
reggie-1 and -2 with Thy-1, GM1, the T-cell receptor complex and fyn.
This, and the accumulation of reggie proteins in detergent-resistant membrane fractions containing F3, Thy-1, and fyn imparts to reggie-1 and -2 properties of raft-associated proteins. It also suggests that
reggie-1 and -2 participate in the formation of signal transduction centers. In addition, we find reggie-1 and -2 in endolysosomes. In
Jurkat cells, reggie-1 and -2 together with fyn and Thy-1 increase in
endolysosomes concurrent with a decrease at the plasma membrane. Thus,
reggie-1 and -2 define raft-related microdomain signaling centers in
neurons and T cells, and the protein complex involved in signaling
becomes subject to degradation.
Present address: Dr. Dirk M. Lang, Department of
Human Biology, Faculty of Health Sciences, University of Cape Town,
Observatory 7925, Cape Town, Republic of South Africa. E-mail address:
dlang{at}cormack.uct.ac.za.
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