The architectural relationship of components controlling mast cell endocytosis

Cleyrat, Cédric; Darehshouri, Anza; Anderson, Karen; Page, Christopher; Lidke, Diane S.; Volkmann, Niels; Hanein, Dorit; Wilson, Bridget S.

doi:10.1242/jcs.128876

Cited by 16 publications

(18 citation statements)

References 63 publications

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“…These clathrincoated sites are unlike those observed by EM in other mammalian cell types (Dambournet et al, 2018;Scott et al, 2018;Sochacki et al, 2014). However, there is some similarity between the raised clathrin structures we observe in B cells and the structures that form on mast cells in response to FCeRI clustering (Aggeler and Werb, 1982;Cleyrat et al, 2013;Wilson et al, 2002). There is overlap in the BCR and FCeRI signaling cascades (Siraganian et al, 2010), and the morphological similarity we observe in the receptors' endocytic structures suggests that there may be commonalities in their mechanisms of internalization as well.…”

Section: Discussionmentioning

confidence: 48%

Structurally distinct endocytic pathways for B cell receptors in B lymphocytes

Davenport

Dickey

Ahn

et al. 2018

Preprint

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B lymphocytes play a critical role in adaptive immunity. Upon antigen binding, B cell receptors (BCR) cluster on the plasma membrane and are internalized by endocytosis. B cells capture diverse antigens in various contexts and concentrations. However, it is unclear whether the mechanism of BCR endocytosis changes in response to these factors. Here, we studied the concentration dependence of anti-human IgM Fab'2-induced BCR clustering and internalization in the human IgM+ DG-75 B cell line using advanced imaging methods, including correlative super resolution fluorescence and electron microscopy. By directly visualizing nanoscale structures associated with BCR clusters, we provide evidence that BCR cluster size increases with Fab'2 concentration and the mechanism of internalization switches in response to BCR cluster size. At low concentrations of Fab'2, B cells internalize BCR clusters by classical clathrin-mediated endocytosis. However, at high Fab'2 concentrations, B cells retrieve clathrin-bound BCR clusters using large invaginations of the plasma membrane.

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Section: Discussionmentioning

confidence: 48%

Structurally distinct endocytic pathways for B cell receptors in B lymphocytes

Davenport

Dickey

Ahn

et al. 2018

Preprint

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“…Stable transfectants were obtained using the appropriate selective agent as described in Cleyrat et al[53]…”

Section: Experimental Methodsmentioning

confidence: 99%

Three dimensional time-gated tracking of non-blinking quantum dots in live cells

et al. 2015

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Single particle tracking has provided a wealth of information about biophysical processes such as motor protein transport and diffusion in cell membranes. However, motion out of the plane of the microscope or blinking of the fluorescent probe used as a label generally limits observation times to several seconds. Here, we overcome these limitations by using novel non-blinking quantum dots as probes and employing a custom 3D tracking microscope to actively follow motion in three dimensions (3D) in live cells. Signal-to-noise is improved in the cellular milieu through the use of pulsed excitation and time-gated detection.

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“…However, two independent groups have more recently reported that siRNA-mediated clathrin depletion does not affect antigen-dependent FcεRI internalization (65, 75), demonstrating that engaged FcεRI complexes can efficiently take an alternative route for endocytosis if the clathrin pathway is inhibited.…”

Section: The Ubiquitin Pathway As Endocytic Route Of Fc Receptorsmentioning

confidence: 99%

Regulation of Fc Receptor Endocytic Trafficking by Ubiquitination

et al. 2014

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Most immune cells, particularly phagocytes, express various receptors for the Fc portion of the different immunoglobulin isotypes (Fc receptors, FcRs). By binding to the antibody, they provide a link between the adaptive immune system and the powerful effector functions triggered by innate immune cells such as mast cells, neutrophils, macrophages, and NK cells. Upon ligation of the immune complexes, the downstream signaling pathways initiated by the different receptors are quite similar for different FcR classes leading to the secretion of preformed and de novo synthesized pro-inflammatory mediators. FcR engagement also promotes negative signals through the combined action of several molecules that limit the extent and duration of positive signaling. To this regard, ligand-induced ubiquitination of FcRs for IgE (FcεR) and IgG (FcγR) has become recognized as a key modification that generates signals for the internalization and/or delivery of engaged receptor complexes to lysosomes or cytoplasmic proteasomes for degradation, providing negative-feedback regulation of Fc receptor activity. In this review, we discuss recent advances in our understanding of the molecular mechanisms that ensure the clearance of engaged Fcε and Fcγ receptor complexes from the cell surface with an emphasis given to the cooperation between the ubiquitin pathway and endosomal adaptors including the endosomal sorting complex required for transport (ESCRT) in controlling receptor internalization and sorting along the endocytic compartments.

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The architectural relationship of components controlling mast cell endocytosis

Cited by 16 publications

References 63 publications

Structurally distinct endocytic pathways for B cell receptors in B lymphocytes

Structurally distinct endocytic pathways for B cell receptors in B lymphocytes

Three dimensional time-gated tracking of non-blinking quantum dots in live cells

Regulation of Fc Receptor Endocytic Trafficking by Ubiquitination

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