RT info:eu-repo/semantics/article
T1 WIP regulates signaling via the high affinity receptor for immunoglobulin E in mast cells
A1 Kettner, Alexander
A1 Kumar, Lalit
A1 Antón, Inés María
A1 Sasahara, Yoji
A1 Fuente García, Miguel Ángel de la
A1 Pivniouk, Vadim
A1 Falet, Hervé
A1 Hartwig, John H.
A1 Geha, Raif S.
K1 Síndrome de Wiskott-Aldrich
AB Wiskott-Aldrich syndrome protein-interacting protein (WIP) stabilizes actin filaments and is important for immunoreceptor-mediated signal transduction leading to actin cytoskeleton rearrangement in T and B cells. Here we report a role for WIP in signaling pathways downstream of the high affinity receptor for immunoglobulin (Ig)E (FcepsilonRI) in mast cells. WIP-deficient bone marrow-derived mast cells (BMMCs) were impaired in their capacity to degranulate and secrete interleukin 6 after FcepsilonRI ligation. Calcium mobilization, phosphorylation of Syk, phospholipase C-g2, and c-Jun NH2-terminal kinase were markedly decreased in WIP-deficient BMMCs. WIP was found to associate with Syk after FcepsilonRI ligation and to inhibit Syk degradation as evidenced by markedly diminished Syk levels in WIP-deficient BMMCs. WIP-deficient BMMCs exhibited no apparent defect in their subcortical actin network and were normal in their ability to form protrusions when exposed to an IgE-coated surface. However, the kinetics of actin changes and the cell shape changes that follow FcepsilonRI signaling were altered in WIP-deficient BMMCs. These results suggest that WIP regulates FcepsilonRI-mediated mast cell activation by regulating Syk levels and actin cytoskeleton rearrangement.
PB Rockefeller University Press
SN 0022-1007
YR 2004
FD 2004
LK http://uvadoc.uva.es/handle/10324/10125
UL http://uvadoc.uva.es/handle/10324/10125
LA eng
NO Journal of Experimental Medicine, 2004, vol. 199, n. 3. p. 357-368
NO Producción Científica
DS UVaDOC
RD 26-dic-2024