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

Kwiatkowska K, Frey J, Sobota A (2003)
JOURNAL OF CELL SCIENCE 116(3): 537-550.

Zeitschriftenaufsatz | Veröffentlicht| Englisch
 
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Autor/in
Kwiatkowska, K; Frey, JürgenUniBi; Sobota, A
Abstract / Bemerkung
Activation of Fey receptor II (FcgammaRII) induces rearrangement of the actin-based cytoskeleton that serves as a driving force for FcgammaRII-mediated phagocytosis and FcgammaRII 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 FcgammaRII in U937 cells. After crosslinking, FcgammaRII 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 FcgammaRII was diminished and assembly of FcgammaRH caps was blocked. The similar reduction of FcgammaRH 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 FcgammaRIIA expressed in BHK cells, lacking endogenous FcgammaRs, 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 wildtype FcgammaRHA. On the basis of these data, we suggest that tyrosine phosphorylation of activated FcgammaRIIA by raft-residing tyrosine kinases of the Src family triggers signaling pathways that control the rearrangement of the actin cytoskeleton required for FcgammaRH-mediated motility.
Stichworte
Fc gamma receptor II; Lyn; actin cytoskeleton; capping; membrane rafts
Erscheinungsjahr
2003
Zeitschriftentitel
JOURNAL OF CELL SCIENCE
Band
116
Ausgabe
3
Seite(n)
537-550
ISSN
0021-9533
eISSN
1477-9137
Page URI
https://pub.uni-bielefeld.de/record/1612549

Zitieren

Kwiatkowska K, Frey J, Sobota A. Phosphorylation of Fc gamma RIIA is required for the receptor-induced actin rearrangement and capping: the role of membrane rafts. JOURNAL OF CELL SCIENCE. 2003;116(3):537-550.
Kwiatkowska, K., Frey, J., & Sobota, A. (2003). Phosphorylation of Fc gamma RIIA is required for the receptor-induced actin rearrangement and capping: the role of membrane rafts. JOURNAL OF CELL SCIENCE, 116(3), 537-550. doi:10.1242/jcs.00254
Kwiatkowska, K., Frey, J., and Sobota, A. (2003). Phosphorylation of Fc gamma RIIA is required for the receptor-induced actin rearrangement and capping: the role of membrane rafts. JOURNAL OF CELL SCIENCE 116, 537-550.
Kwiatkowska, K., Frey, J., & Sobota, A., 2003. Phosphorylation of Fc gamma RIIA is required for the receptor-induced actin rearrangement and capping: the role of membrane rafts. JOURNAL OF CELL SCIENCE, 116(3), p 537-550.
K. Kwiatkowska, J. Frey, and A. Sobota, “Phosphorylation of Fc gamma RIIA is required for the receptor-induced actin rearrangement and capping: the role of membrane rafts”, JOURNAL OF CELL SCIENCE, vol. 116, 2003, pp. 537-550.
Kwiatkowska, K., Frey, J., Sobota, A.: Phosphorylation of Fc gamma RIIA is required for the receptor-induced actin rearrangement and capping: the role of membrane rafts. JOURNAL OF CELL SCIENCE. 116, 537-550 (2003).
Kwiatkowska, K, Frey, Jürgen, and Sobota, A. “Phosphorylation of Fc gamma RIIA is required for the receptor-induced actin rearrangement and capping: the role of membrane rafts”. JOURNAL OF CELL SCIENCE 116.3 (2003): 537-550.

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