Palmitoylation is required for efficient Fas cell death signaling

Chakrabandhu, Krittalak; Hérincs, Zoltán; Huault, Sébastien; Dost, Britta; Peng, Ling; Conchonaud, Fabien; Marguet, Didier; He, Hai-Tao; Hueber, Anne-Odile

doi:10.1038/sj.emboj.7601456

Cited by 165 publications

(172 citation statements)

References 45 publications

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“…Increased Fas-induced apoptosis caused by ezrin knockdown was found in normal lymphocytes and H9 cells, but not in Jurkat and CEM cells. In contrast to reports that ezrin is essential for Fas-initiated apoptosis (Parlato et al, 2000;Piazzolla et al, 2005;Chakrabandhu et al, 2007;He´bert et al, 2008), our results support an alternative view that ezrin inactivation and dissociation from actin enhance Fas-induced cell death (Kondo et al, 1997;Ramaswamy et al, 2007). The opposite results found for the function of ezrin were unlikely to be due to the use of different reagents; the ezrin-specific siRNA used in this study was identical to that used in a recent study illustrating the positive effect of ezrin in Fas-triggered apoptosis in Jurkat cells (He´bert et al, 2008).…”

Section: Discussionmentioning

confidence: 59%

“…Internalization of Fas is required for efficient DISC formation and caspase-8 activation (Lee et al, 2006;Chakrabandhu et al, 2007). Ezrin-actin association is reported to be required for endocytosis of Fas in mouse embryonic fibroblasts and L12.10 cells (Piazzolla et al, 2005;Chakrabandhu et al, 2007Chakrabandhu et al, , 2008.…”

Section: Discussionmentioning

confidence: 99%

“…Normal Fas endocytosis in ezrin-deficient H9 cells after Fas engagement Another reported function of ezrin is its involvement in the endocytosis of Fas that is essential for DISC formation and the activation of caspase-8 (Lee et al, 2006;Chakrabandhu et al, 2007). We analysed whether the internalization of Fas was affected by ezrin deficiency in H9 cells.…”

Section: Deficiency In Ezrin Enhancesmentioning

confidence: 99%

“…Depending on the amount of DISC formation, Fas-sensitive cells are divided into type I and type II (Scaffidi et al, 1998). In type I cells, Fas forms sodium dodecyl sulfate-resistant high-order aggregates, followed by rapid internalization of Fas and DISC formation (Algeciras-Schimnich et al, 2002;Lee et al, 2006;Chakrabandhu et al, 2007;Feig et al, 2007). In type II cells, a very limited amount of DISC is formed and apoptotic signaling needs amplification through mitochondria (Scaffidi et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

“…The downregulation of ezrin in CEM cells abolishes their susceptibility to Fas-induced apoptosis (Parlato et al, 2000), and the knockdown of ezrin or moesin in Jurkat cells decreases Fas-triggered apoptosis (He´bert et al, 2008). It has also been shown that Fasezrin-actin linkage is involved in Fas endocytosis, and Fas-induced apoptosis was attenuated in ezrin-knockdown L12.10 cells (Chakrabandhu et al, 2007(Chakrabandhu et al, , 2008. Therefore, the exact role of ezrin in death receptorinitiated apoptosis remains unsettled.…”

Section: Introductionmentioning

confidence: 99%

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Ezrin is a negative regulator of death receptor-induced apoptosis

et al. 2009

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Ezrin links cortical actin filaments with the cell membrane, and has a critical role in many membrane-initiated events. Fas is directly associated with ezrin, but conflicting results have been reported for the involvement of ezrin in Fas-induced cell death. In this study we show that ezrin was associated with Fas in T cells before stimulation and was released shortly after Fas ligand (FasL) engagement. The knockdown of ezrin moderately increased Fastriggered or tumor necrosis factor-related apoptosisinducing ligand (TRAIL)-triggered cell death in normal T lymphocytes and in H9 cells, but had no effect on death receptor-induced apoptosis in type II cells, such as Jurkat and CEM. Expression of a dominant-negative form of ezrin also led to an increased Fas-induced apoptosis in H9 cells. Ezrin deficiency did not affect the internalization of Fas after Fas ligation. Instead, an enhanced formation of death-inducing signaling complex (DISC) was observed in H9 cells with ezrin knockdown, leading to accelerated caspase-8 activation. Together, our results suggest that ezrin has a negative role in the recruitment of Fas into signaling complexes in type I T cells. Loss of ezrin likely removes the constraint imposed by ezrin and facilitates the assembly of death receptor complex in T cells.

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Section: Discussionmentioning

confidence: 59%

Section: Discussionmentioning

confidence: 99%

Section: Deficiency In Ezrin Enhancesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Ezrin is a negative regulator of death receptor-induced apoptosis

et al. 2009

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Fas/FasL

Guicciardi¹,

Gores²

2015

Signaling Pathways in Liver Diseases

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Characterization of the plasma membrane dynamics during cell signaling processes investigated by spot variation fluorescence correlation spectroscopy ( svFCS )

Mailfert

Hamon

et al. 2016

European Microscopy Congress 2016: Proceedings

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The plasma membrane organization is highly heterogeneous as a result of the intrinsic molecular Brownian agitation and the vast diversity of membrane components. Selective interactions take place in the formation of local complex multicomponent assemblies of lipids and proteins on different time scales. Still, deciphering this lateral organization on living cells and on the appropriate length and temporal scales has been challenging but is crucial to advance our knowledge on the biological function of the plasma membrane. Among the methodological developments made during the last decade, the spot variation FCS (svFCS), a fluorescent correlation spectroscopy (FCS)‐based method, has allowed the significant progress in the characterization of cell membrane lateral organization at the sub‐optical level, including to providing compelling evidence for the in vivo existence of lipid‐dependent nanodomains (see for review ) 1 .This method provides particular insight to identify possible molecular confinement occurring at the plasma membrane 1, 2 . The svFCS is performed by changing the spot of illumination underfilling the back aperture of the objective 3 . Theoretical models have been developed to predict how geometrical constraints such as the presence of adjacent or isolated domains affect the svFCS observations 4, 5 . We will illustrate how the investigations based on svFCS have provided compelling evidence for the in vivo existence of lipid‐dependent nanodomains 2, 6, 7 and have allowed significant progress in the characterization of cell membrane lateral organization for different kind of receptors 8‐10 .

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Palmitoylation is required for efficient Fas cell death signaling

Cited by 165 publications

References 45 publications

Ezrin is a negative regulator of death receptor-induced apoptosis

Ezrin is a negative regulator of death receptor-induced apoptosis

Fas/FasL

Characterization of the plasma membrane dynamics during cell signaling processes investigated by spot variation fluorescence correlation spectroscopy ( svFCS )

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