Anthrax toxin triggers endocytosis of its receptor via a lipid raft–mediated clathrin-dependent process

Abrami, Laurence; Liu, Shihui; Cosson, Pierre; Leppla, Stephen H.; Goot, F. Gisou van der

doi:10.1083/jcb.200211018

Cited by 449 publications

(489 citation statements)

References 47 publications

(67 reference statements)

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“…When clathrin-coated pits are pinched off from the plasma membrane, the free clathrin-coated vesicles rap- idly lose their clathrin coats through a process mediated by Hsc70 and auxilin [41][42][43]. Still, clathrin-coated vesicles can be frequently observed underneath the plasma membrane as shown in this study and previous reports [44,45].…”

Section: During the Infection Of Viruses Such As Simian Virussupporting

confidence: 66%

Internalization of the TGF-β type I receptor into caveolin-1 and EEA1 double-positive early endosomes

Yan

et al. 2015

Cell Res

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Endocytosis and intracellular sorting of transforming growth factor-β (TGF-β) receptors play an important regulatory role in TGF-β signaling. Two major endocytic pathways, clathrin-and caveolae-mediated endocytosis, have been reported to independently mediate the internalization of TGF-β receptors. In this study, we demonstrate that the clathrin-and caveolae-mediated endocytic pathways can converge during TGF-β receptor endocytic trafficking. By tracking the intracellular dynamics of fluorescently-labeled TGF-β type I receptor (TβRI), we found that after mediating TβRI internalization, certain clathrin-coated vesicles and caveolar vesicles are fused underneath the plasma membrane, forming a novel type of caveolin-1 and clathrin double-positive vesicles. Under the regulation of Rab5, the fused vesicles are targeted to early endosomes and thus deliver the internalized TβRI to the caveolin-1 and EEA1 double-positive early endosomes (caveolin-1-positive early endosomes). We further showed that the caveolin-1-positive early endosomes are positive for Smad3/SARA, Rab11 and Smad7/Smurf2, and may act as a multifunctional device for TGF-β signaling and TGF-β receptor recycling and degradation. Therefore, these findings uncover a novel scenario of endocytosis, the direct fusion of clathrin-coated and caveolae vesicles during TGF-β receptor endocytic trafficking, which leads to the formation of the multifunctional sorting device, caveolin-1-positive early endosomes, for TGF-β receptors.

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Section: During the Infection Of Viruses Such As Simian Virussupporting

confidence: 66%

Internalization of the TGF-β type I receptor into caveolin-1 and EEA1 double-positive early endosomes

Yan

et al. 2015

Cell Res

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“…The flexible loop of PA domain 2 partially detaches from the monomer and associates with the six other loops of the neighbouring monomers to form a β-barrel that inserts into the membrane, similar to α-haemolysin and leukocidin from S. aureus. Interestingly, leukocidins are also binary toxins involved in pore formation, but remain on the cell surface, whereas PA enables the translocation of partially unfolded enzymatic components into the cytosol through a pH gradient (Blöcker et al, 2001;Marvaud et al, 2001;Cunningham et al, 2002;Mogridge et al, 2002aMogridge et al, , 2002bAbrami et al, 2003).…”

Section: B Geny and Mr Popoffmentioning

confidence: 99%

Bacterial protein toxins and lipids: pore formation or toxin entry into cells

Geny

Popoff

2006

Biology of the Cell

118

104

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Lipids are hydrophobic molecules which play critical functions in cells, in particular, they are essential constituents of membranes, whereas bacterial toxins are mainly hydrophilic proteins. All bacterial toxins interact first with their target cells by recognizing a surface receptor, which is either a lipid or a lipid derivative, or another compound but in a lipid environment. Most bacterial toxins are PFTs (pore‐forming toxins) which oligomerize and insert into the lipid bilayer. A common mechanism of action involves the formation of a β‐barrel structure, resulting from the assembly of individual β‐hairpin(s) from individual monomers. An essential step for intracellular active toxins is to translocate their enzymatic part into the cytosol. Some toxins use a translocation mechanism based on pore formation similar to that of PFTs, others undergo a yet unclear ‘chaperone’ process.

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“…These domains have been implicated in several key cellular functions such as signaling, endocytosis, polarization (Simons and Toomre, 2000). Raft domains have also been shown to be the entry points for viruses (Campbell et al, 2001) and toxins (Lencer, 2001) and to act as pathogenic platforms for conversion of the cellular prion (PrP c ) to the scrapie version (PrP sc ) (Hooper, 2005), for bcleavage of the amyloid precursor protein (APP) (Ehehalt et al, 2003), and for activation of anthrax toxin (Abrami et al, 2003;Kurzchalia, 2003).…”

Section: Introductionmentioning

confidence: 99%

Raft association and lipid droplet targeting of flotillins are independent of caveolin

Rajendran

Lay

Illges

2007

Biological Chemistry

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Lipid rafts are liquid ordered platforms that dynamically compartmentalize membranes. Caveolins and flotillins constitute a group of proteins that are enriched in these domains. Caveolin-1 has been shown to be an essential component of caveolae. Flotillins were also discovered as an integral component of caveolae and have since been suggested to interact with caveolins. However, flotillins are also expressed in non-caveolae-containing cells such as lymphocytes and neuronal cells. Hence, a discrepancy exists in the literature regarding the caveolin dependence of flotillin expression and their subcellular localization. To address this controversy, we used mouse embryonic fibroblasts (MEFs) from caveolin-1 knockout (Cav-1 -/-) and wild-type mice to study flotillin expression and localization. Here we show that both membrane association and lipid raft partitioning of flotillins are not perturbed in Cav-1 -/-MEFs, whereas membrane targeting and raft partitioning of caveolin-2, another caveolin family protein, is severely impaired. Moreover, we demonstrate that flotillin-1, but not flotillin-2, associates with lipid droplets upon oleic acid treatment and that this association is completely independent of caveolin. Taken together, our results show that flotillins are localized in lipid rafts independent of caveolin-1 and that translocation of flotillin-1 to lipid droplets is a caveolin-independent process.

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Anthrax toxin triggers endocytosis of its receptor via a lipid raft–mediated clathrin-dependent process

Cited by 449 publications

References 47 publications

Internalization of the TGF-β type I receptor into caveolin-1 and EEA1 double-positive early endosomes

Internalization of the TGF-β type I receptor into caveolin-1 and EEA1 double-positive early endosomes

Bacterial protein toxins and lipids: pore formation or toxin entry into cells

Raft association and lipid droplet targeting of flotillins are independent of caveolin

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