Signaling assemblies formed in mast cells activated via Fcϵ receptor I dimers

Dráberová, Lubica; Lebduška, Pavel; Hálová, Ivana; Tolar, Pavel; Štokrová, Jitka; Tolarová, Helena; Korb, J; Dráber, Petr

doi:10.1002/eji.200322663

Cited by 22 publications

(27 citation statements)

References 24 publications

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“…Although pretreatment with latrunculin did not affect association of several signaling proteins (Lyn, LAT, NTAL and Thy-1) with DRM, it enhanced tyrosine phosphorylation of LAT, NTAL and even Syk, which is not considered to be associated with lipid rafts. It should be noted, however, that Syk could be recruited to lipid rafts through its binding to lipid raftresiding molecules such as Lyn [28] or aggregated FceRI [10,12]. The combined data support the notion that actin cytoskeleton is involved in setting the threshold for activation of mast cells through various pathways.…”

Section: Cross-talk Between Thy-1 and Fcerisupporting

confidence: 59%

“…Based on these results, Wilson and co-authors suggested that the observed FceRI aggregates could represent the true signal transduction organizing units [14]. However, we recently found that mAb-mediated FceRI dimerization induces strong cell activation response in the absence of formation of the large signaling assemblies around FceRI aggregates [12]. Thus, FceRI signal transduction units could be much smaller than previously thought [14,16], and their molecular topography and changes during the course of mast cell activation remain enigmatic.…”

Section: Introductionmentioning

confidence: 79%

“…However, EM observations failed to discern any significant increase in association between Thy-1 and aggregated FceRI [12,15]. To elucidate these discrepancies, we further investigated the topography of Thy-1 and FceRI by means of FRET, a method with 1-10 nm resolution.…”

Section: Cross-talk Between Thy-1 and Fcerimentioning

confidence: 99%

“…Biochemical studies with detergent-solubilized cells implied that FceRI-mediated activation is initiated by coalescence of aggregated FceRI with DRM [10,12] and that F-actin is involved in this process [19,20]. However, EM observations failed to discern any significant increase in association between Thy-1 and aggregated FceRI [12,15].…”

Section: Cross-talk Between Thy-1 and Fcerimentioning

confidence: 99%

“…Biochemical studies of isolated detergent-resistant membranes (DRM) showed that they are rich not only in GPI-anchored proteins, but also in palmitoylated Src family protein tyrosine kinases [6,7] and palmitoylated transmembrane adaptor proteins, including linker for activation of T cells (LAT) [8] and non-T cell activation linker (NTAL) [9]. Importantly, in nonactivated mast cells, the FceRI is excluded from DRM, whereas in FceRI-activated cells most of the receptor is associated with DRM in a cholesterol-dependent manner [10][11][12]. These findings suggested that FceRI-mediated activation is initiated through association of the aggregated FceRI with membrane microdomains possessing signal transduction machinery.…”

Section: Introductionmentioning

confidence: 99%

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Topography of plasma membrane microdomains and its consequences for mast cell signaling

et al. 2006

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Thy-1 (CD90) is a glycoprotein bound to the plasma membrane by a GPI anchor. Aggregation of Thy-1 in mast cells and basophils induces activation events independent of the expression of Fce receptor I (FceRI). Although we and others have previously suggested that plasma membrane microdomains called lipid rafts are implicated in both Thy-1 and FceRI signaling, properties of these microdomains are still poorly understood. In this study we used rat basophilic leukemia cells and their transfectants expressing both endogenous Thy-1.1 and exogenous Thy-1.2 genes and analyzed topography of the Thy-1 isoforms and Thy-1-induced signaling events. Light microscopy showed that both Thy-1 isoforms were in the plasma membrane distributed randomly and independently. Electron microscopy on isolated membrane sheets and fluorescence resonance energy transfer analysis indicated cross-talk between Thy-1 isoforms and between Thy-1 and FceRI. This cross-talk was dependent on actin filaments. Thy-1 aggregates colocalized with two transmembrane adaptor proteins, non-T cell activation linker (NTAL) and linker for activation of T cells (LAT), which had been shown to inhabit different membrane microdomains. Thy-1 aggregation led to tyrosine phosphorylation of these two adaptors. The combined data indicate that aggregated GPI-anchored proteins can attract different membrane proteins in different clusters and thus can trigger different signaling pathways.

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Section: Cross-talk Between Thy-1 and Fcerisupporting

confidence: 59%

Section: Introductionmentioning

confidence: 79%

Section: Cross-talk Between Thy-1 and Fcerimentioning

confidence: 99%

Section: Cross-talk Between Thy-1 and Fcerimentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Topography of plasma membrane microdomains and its consequences for mast cell signaling

et al. 2006

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Signaling Chain Homooligomerization (SCHOOL) Model

Sigalov

Advances in Experimental Medicine and Biology

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Multichain immune recognitionreceptors (MIRRs) represent a family of surfacereceptors expressed on different cells of the hematopoietic system and function to transduce signals leading to a variety of biologic responses. The most intriguing and distinct structural feature ofMIRR family members is that extracellular recognition domains and intracellular signaling domains are located on separate subunits. The biochemical cascades triggered by MIRRs are understood in significant detail, however, the mechanism by which extracellular ligand binding initiates intracellular signal transduction processes is not clear and no model fully explains how MIRR signaling commences. In this Chapter, I describe a novel mechanistic model of MIRR-mediated signal transduction, the signaling chain homooligomerization (SCHOOL) model. The basic concept of this model assumes that the structural similarity of the MIRRs provides the basis for the similarity in the mechanisms ofMIRR-mediated transmembrane signaling. Within the SCHOOL model, MIRR triggering is considered to be a result of the ligand-induced interplay between (1) intrareceptor transmembrane interactions between MIRR recognition and signaling subunits that stabilize and maintain receptor integrity and (2) interreceptor homointeractions between MIRR signaling subunits that lead to the formation of oligomeric signaling structures, thus triggering the receptors and initiating the signaling cascade. Thus, the SCHOOL model is based on specific protein-protein interactions--biochemical processes that can be influenced and controlled. In this context, this plausible and easily testable model is fundamentally different from those previously suggested for particular MIRRs and has several important advantages. The basic principles oftransmembrane signaling learned from the SCHOOL model may be used in different fields of immunology and cell biology to describe, explain and predict immunological phenomena and processes mediated by structurally related but functionally different membrane receptors. Important applications of the SCHOOL model in clinical immunology, molecular pharmacology and virology are described in the Chapters 20 and 22 of this book.

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Membrane-Cytoskeleton Dynamics in the Course of Mast Cell Activation

Dráber

2014

Mast Cells

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Aggregation of the high-affinity IgE receptor (FcεRI) on the plasma membrane of mast cells and basophils initiates signaling events leading to a rapid release of preformed inflammatory mediators from secretory granules, and overall changes in cell morphology. Mast cell activation also causes reorganization of cytoskeletal components associated with membrane ruffling, spreading, and migration. Here we describe methods used for visualization of mast cell cytoskeleton, focusing on its two major components, microfilaments and microtubules, and their changes after cell triggering.

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Signaling assemblies formed in mast cells activated via Fcϵ receptor I dimers

Cited by 22 publications

References 24 publications

Topography of plasma membrane microdomains and its consequences for mast cell signaling

Topography of plasma membrane microdomains and its consequences for mast cell signaling

Signaling Chain Homooligomerization (SCHOOL) Model

Membrane-Cytoskeleton Dynamics in the Course of Mast Cell Activation

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