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JCS ePress online publication date 11 Dec 2002
doi: 10.1242/jcs.00254

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Research Article

Phosphorylation of Fc{gamma}RIIA is required for the receptor-induced actin rearrangement and capping: the role of membrane rafts


Katarzyna Kwiatkowska, Jürgen Frey, and Andrzej Sobota*
* Author for correspondence (e-mail: asobota{at}nencki.gov.pl)

Activation of Fc{gamma} receptor II (Fc{gamma}RII) induces rearrangement of the actin-based cytoskeleton that serves as a driving force for Fc{gamma}RII-mediated phagocytosis and Fc{gamma}RII 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 Fc{gamma}RII in U937 cells. After crosslinking, Fc{gamma}RII 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-{alpha}-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 {beta}-cyclodextrin. Under these conditions, phosphorylation of the crosslinked Fc{gamma}RII was diminished and assembly of Fc{gamma}RII caps was blocked. The similar reduction of Fc{gamma}RII 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 Fc{gamma}RIIA expressed in BHK cells, lacking endogenous Fc{gamma}Rs, 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 Fc{gamma}RIIA. On the basis of these data, we suggest that tyrosine phosphorylation of activated Fc{gamma}RIIA by raft-residing tyrosine kinases of the Src family triggers signaling pathways that control the rearrangement of the actin cytoskeleton required for Fc{gamma}RII-mediated motility.




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