PtdIns(4,5)P-restricted plasma membrane localization of FAN is involved in TNF-induced actin reorganization

Haubert, Dirk; Gharib, Nina; Rivero, Francisco; Wiegmann, Katja; Hösel, Marianna; Krönke, Martin; Kashkar, Hamid

doi:10.1038/sj.emboj.7601778

Cited by 32 publications

(46 citation statements)

References 78 publications

(104 reference statements)

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“…Although the connection between p75 and RhoA is well understood (see above), it remains to be discovered how other TNFRs link to small GTPases. As discussed above, death-domain-binding adaptors are not necessarily required to mediate Cdc42 activation and cytoskeletal changes (Puls et al, 1999), and molecules such as FAN that transmit signals from the TNFR to the cytoskeleton and bind to other parts of the intracellular domain of the TNFR are now being identified (Haubert et al, 2007) (Fig. 4).…”

Section: A Morphogenetic Signalling Pathway?mentioning

confidence: 99%

“…Furthermore, certain TNFα-dependent effects on the cytoskeleton do not require the receptor's death domain (Peppelenbosch et al, 1999), but instead require a more membraneproximal region of the receptor, the neutral sphingomyelinase (NSMase)-activating domain (Adam-Klages et al, 1996). One adaptor protein, factor associated with N-SMase activity (FAN), which binds to this region, is required for TNFα-dependent activation of Cdc42 and filopodium formation (Haubert et al, 2007). Other molecules that have been implicated in TNFα-stimulated modulation of GTPases include MAP kinases, phosphoinositide 3-kinases, PLCγ1 and ceramide (Hanna et al, 2001;Kutsuna et al, 2004;Papakonstanti and Stournaras, 2004).…”

Section: Tnfα Modulates the Cytoskeleton Via Rho-family Gtpasesmentioning

confidence: 99%

“…The pro-inflammatory effects of TNFα treatment on cultured cells and the associated effects on the cytoskeleton are summarized in Table 1. Recent studies have directly demonstrated effects of TNF signalling on cytoskeletal rearrangements and other morphogenetic processes (Corredor et al, 2003;Haubert et al, 2007;Kutsuna et al, 2004;Lokuta and Huttenlocher, 2005;McKenzie and Ridley, 2007). Thus, cells treated with TNF can be induced to migrate (Postlethwaite and Seyer, 1990) or undergo cell-shape changes that are not normally associated with apoptosis (Puls et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

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Looking beyond death: a morphogenetic role for the TNF signalling pathway

Mathew

Haubert

Krönke

et al. 2009

Journal of Cell Science

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Tumour necrosis factor α (TNFα) is a pro-inflammatory mediator with the capacity to induce apoptosis. An integral part of its apoptotic and inflammatory programmes is the control of cell shape through modulation of the cytoskeleton, but it is now becoming apparent that this morphogenetic function of TNF signalling is also employed outside inflammatory responses and is shared by the signalling pathways of other members of the TNF-receptor superfamily. Some proteins that are homologous to the components of the TNF signalling pathway, such as the adaptor TNF-receptor-associated factor 4 and the ectodysplasin A receptor (and its ligand and adaptors), have dedicated morphogenetic roles. The mechanism by which TNF signalling affects cell shape is not yet fully understood, but Rhofamily GTPases have a central role. The fact that the components of the TNF signalling pathway are evolutionarily old suggests that an ancestral cassette from unicellular organisms has diversified its functions into partly overlapping morphogenetic, inflammatory and apoptotic roles in multicellular higher organisms.

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Section: A Morphogenetic Signalling Pathway?mentioning

confidence: 99%

Section: Tnfα Modulates the Cytoskeleton Via Rho-family Gtpasesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Looking beyond death: a morphogenetic role for the TNF signalling pathway

Mathew

Haubert

Krönke

et al. 2009

Journal of Cell Science

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“…54 PH domains are generally involved in interaction with phosphoinositides or mediate protein-protein interactions. The PH-like domain of the small human BEACH protein factor associated with neural sphingomyelinase (FAN) is shown to bind PI(4,5)P2, 55 but it is not known whether the PH-like domain of ALFY is functional. The PH-like and WD40 domains show a moderate degree of conservation throughout human BEACH proteins whereas the BEACH domain is highly conserved.…”

Section: Adaptor Proteinsmentioning

confidence: 99%

The role of ALFY in selective autophagy

2012

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Autophagy, a highly conserved lysosomal degradation pathway, was initially characterized as a bulk degradation system induced in response to starvation. In recent years, autophagy has emerged also as a highly selective pathway, targeting various cargoes such as aggregated proteins and damaged organelles for degradation. The key factors involved in selective autophagy are autophagy receptors and adaptor proteins, which connect the cargo to the core autophagy machinery. In this review, we discuss the current knowledge about the only mammalian adaptor protein identified thus far, autophagy-linked FYVE protein (ALFY). ALFY is a large, scaffolding, multidomain protein implicated in the selective degradation of ubiquitinated protein aggregates by autophagy. We also comment on the possible role of ALFY in the context of disease.

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“…Involvement of PA Binding to the PH Domain in the Localization of RA-RhoGAP at Plasma Membrane-It has been reported that PH domain-containing proteins localize at the membrane by binding of the PH domains to phospholipids (35,43). Therefore, we examined whether binding of the PH domain of RA-RhoGAP to PA was responsible for membrane localization.…”

Section: Volume 286 • Number 8 • February 25 2011mentioning

confidence: 99%

Dual Regulation of RA-RhoGAP Activity by Phosphatidic Acid and Rap1 during Neurite Outgrowth

Kurooka

Yamamoto

Takai

et al. 2011

Journal of Biological Chemistry

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During neurite outgrowth, Rho small G protein activity is spatiotemporally regulated to organize the neurite sprouting, extension, and branching. We have previously identified a potent Rho GTPase-activating protein (GAP), RA-RhoGAP, as a direct downstream target of Rap1 small G protein in the neurite outgrowth. In addition to the Ras-associating (RA) domain for Rap1 binding, RA-RhoGAP has the pleckstrin homology (PH) domain for lipid binding. Here, we showed that phosphatidic acid (PA) bound to the PH domain and enhanced GAP activity for Rho. RA-RhoGAP induced extension of neurite in a diacylglycerol kinase-mediated synthesis of the PA-dependent manner. Knockdown of RA-RhoGAP reduced the diacylglycerol kinase-induced neurite extension. In contrast to the effect of the RA domain, the PH domain was specifically involved in the neurite extension, not in the sprouting and branching. These results indicate that PA and Rap1 cooperatively regulate RA-RhoGAP activity for promoting neurite outgrowth.Formation and extension of axons and dendrites, the socalled neurite outgrowth, are crucial events in neuronal differentiation and maturation during development of the nervous system (1, 2). As neurites extend further and acquire their final axonal and dendritic identities, neurons establish synaptic contacts and reach full maturation (3-5). These morphological changes require remodeling of the actin cytoskeleton (6). Rho small G protein is a key regulator of the actin cytoskeleton organization in neurons and has been shown to play important roles in several aspects of neurite outgrowth, such as sprouting, extension, and branching (7,8). An increase in Rho activity results in reduction of neurite sprouting, extension, and branching, whereas a decrease in Rho activity enhances neurite sprouting, extension, and branching (9 -12). The Rho activity is positively regulated by guanine nucleotide exchange factors (GEFs) 2 and negatively regulated

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PtdIns(4,5)P-restricted plasma membrane localization of FAN is involved in TNF-induced actin reorganization

Cited by 32 publications

References 78 publications

Looking beyond death: a morphogenetic role for the TNF signalling pathway

Looking beyond death: a morphogenetic role for the TNF signalling pathway

The role of ALFY in selective autophagy

Dual Regulation of RA-RhoGAP Activity by Phosphatidic Acid and Rap1 during Neurite Outgrowth

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