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First published online 11 December 2002
doi: 10.1242/jcs.00254
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Research Article |
RIIA is required for the receptor-induced actin rearrangement and capping: the role of membrane rafts
1 Department of Cell Biology, Nencki Institute of Experimental Biology, 3
Pasteur St., 02-093 Warsaw, Poland
2 Universität Bielefeld, Fakultät für Chemie, Biochemie II, 33615
Bielefeld, Germany
* Author for correspondence (e-mail: asobota{at}nencki.gov.pl)
Accepted 21 October 2002
Activation of Fc
receptor II (FcRII) induces rearrangement of
the actin-based cytoskeleton that serves as a driving force for
FcRII-mediated phagocytosis and FcRII capping. To get insight
into the signaling events that lead to the actin reorganization we
investigated the role of raft-associated Src family tyrosine kinases in
capping of FcRII in U937 cells. After crosslinking, FcRII was
found to be recruited to detergent-resistant membrane domains (DRMs), rafts,
where it coexisted with Lyn kinase and underwent tyrosine phosphorylation. Lyn
was displaced from DRMs under the influence of DL-
-hydroxymyristic acid
and 2-bromopalmitic acid, agents blocking N-terminal myristoylation and
palmitoylation of proteins, respectively, and after disruption of DRM
integrity by depletion of plasma membrane cholesterol with
ß-cyclodextrin. Under these conditions, phosphorylation of the
crosslinked FcRII was diminished and assembly of FcRII caps was
blocked. The similar reduction of FcRII cap formation correlated with
inhibition of receptor phosphorylation was achieved with the use of PP1 and
herbimycin A, specific inhibitors of Src family tyrosine kinases.
Phosphorylation of FcRIIA expressed in BHK cells, lacking endogenous
FcRs, was abolished by substitution of tyrosine 298 by phenylalanine in
the ITAM of the receptor. The mutant receptor did not undergo translocation
towards cap-like structures and failed to promote the receptor-mediated
spreading of the cells, as compared to BHK cells transfected with the
wild-type FcRIIA. On the basis of these data, we suggest that tyrosine
phosphorylation of activated FcRIIA by raft-residing tyrosine kinases
of the Src family triggers signaling pathways that control the rearrangement
of the actin cytoskeleton required for FcRII-mediated motility.
Key words: Fc receptor II, Membrane rafts, Lyn, Capping, Actin cytoskeleton
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