Macropinosome formation by tent pole ruffling in macrophages

Condon, Nicholas D.; Heddleston, John M.; Chew, Teng Leong; Luo, Lin; McPherson, Peter S.; Ioannou, Maria S.; Hodgson, Louis; Stow, Jennifer L.; Wall, Adam A.

doi:10.1083/jcb.201804137

Cited by 97 publications

(114 citation statements)

References 45 publications

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“…Recent studies have identified two distinct pathways of macropinocytosis in macrophages, wherein macropinosomes are derived from peripheral ruffles or derived from dorsal ruffles following receptor activation (Condon et al, 2018;Lim et al, 2015). Dorsal ruffles give rise to larger macropinosomes than peripheral ruffles (Condon et al, 2018;Lim et al, 2015). Our previous studies have shown that the majority of macropinosomes from activated macrophages are derived from these dorsal ruffles (Lim et al, 2015).…”

Section: Discussionmentioning

confidence: 87%

“…Macropinosomes are generated from actinmediated ruffling of the PM. Recent studies have identified two distinct pathways of macropinocytosis in macrophages, wherein macropinosomes are derived from peripheral ruffles or derived from dorsal ruffles following receptor activation (Condon et al, 2018;Lim et al, 2015). Dorsal ruffles give rise to larger macropinosomes than peripheral ruffles (Condon et al, 2018;Lim et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

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FcRn mediates fast recycling of endocytosed albumin and IgG from early macropinosomes in primary macrophages

Toh

Louber

Mahmoud

et al. 2019

Journal of Cell Science

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The neonatal Fc receptor (FcRn) rescues albumin and IgG from degradation following endocytosis and thereby extends the half-life of these plasma proteins. However, the pathways for the uptake of these soluble FcRn ligands, and the recycling itinerary of the FcRn-ligand complexes, have not been identified in primary cells. Here, we have defined the recycling of human albumin and IgG in primary mouse macrophages selectively expressing the human FcRn. Albumin is internalised by macropinocytosis; in the absence of FcRn, internalised albumin is rapidly degraded, while in the presence of FcRn albumin colocalises to SNX5-positive membrane domains and is partitioned into tubules emanating from early macropinosomes for delivery in transport carriers to the plasma membrane. Soluble monomeric IgG was also internalised by macropinocytosis and rapidly recycled by the same pathway. In contrast, the fate of IgG bound to surface Fcγ receptors differed from monomeric IgG endocytosed by macropinocytosis. Overall, our findings identify a rapid recycling pathway for FcRn ligands from early macropinosomes to the cell surface of primary cells.

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Section: Discussionmentioning

confidence: 87%

Section: Discussionmentioning

confidence: 99%

FcRn mediates fast recycling of endocytosed albumin and IgG from early macropinosomes in primary macrophages

Toh

Louber

Mahmoud

et al. 2019

Journal of Cell Science

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“…mStr-Rab10 and EGFP-KIF13A/B-tail were co-expressed in COS-7 cells, and their associations were analyzed by co-immunoprecipitation assays with glutathione-Sepharose beads coupled with GST-GFP nanobody, followed by immunoblotting with the antibodies indicated. Sakane et al, 2012) and regulate certain types of Arf6-dependent endocytosis (Condon et al, 2018;Dutta and Donaldson, 2015). In step 2, EE-resident Rab22A, in addition to Rab10, is indispensable for tubular endosome formation (Fig.…”

Section: Discussionmentioning

confidence: 99%

Rab10 regulates tubular endosome formation through KIF13A/B motors

Etoh

Fukuda

2019

Journal of Cell Science

111

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Recycling endosomes are stations that sort endocytic cargoes to their appropriate destinations. Tubular endosomes have been characterized as a recycling endosomal compartment for clathrinindependent cargoes. However, the molecular mechanism by which tubular endosome formation is regulated is poorly understood. In this study, we identified Rab10 as a novel protein localized at tubular endosomes by using a comprehensive localization screen of EGFPtagged Rab small GTPases. Knockout of Rab10 completely abolished tubular endosomal structures in HeLaM cells. We also identified kinesin motors KIF13A and KIF13B as novel Rab10interacting proteins by means of in silico screening. The results of this study demonstrated that both the Rab10-binding homology domain and the motor domain of KIF13A are required for Rab10-positive tubular endosome formation. Our findings provide insight into the mechanism by which the Rab10-KIF13A (or KIF13B) complex regulates tubular endosome formation. This article has an associated First Person interview with the first author of the paper.

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“…The macropinocytic vesicles can then be tracked as they move around the cell. Similar approaches in mammalian cells suggest novel ways of forming and closing macropinocytic cups (Condon et al, 2018).…”

Section: Microscopymentioning

confidence: 99%

Living on soup: macropinocytic feeding in amoebae

Kay¹,

Williams²,

Manton³

et al. 2019

Int. J. Dev. Biol.

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Macropinocytosis is used by a variety of amoebae for feeding on liquid medium. The amoebae project cups and ruffles from their plasma membrane, driven by actin polymerization, and eventually fuse these back to the membrane, entrapping droplets of medium into internal vesicles. These vesicles are of up to several microns in diameter and are processed through the lysosomal digestive system to extract nutrients. Recognizably the same process is used in metazoan cells for a number of medically important purposes, including the pathological growth of cancer cells. We describe the discovery of macropinocytosis in Dictyostelium amoebae, its genetic regulation by the NF1 RasGAP, and the tools available for its investigation. Work on Dictyostelium over the last 30 years has identified many genes that may be important for macropinocytosis, which are listed at dictyBase, and give a basis for mechanistic studies. We argue that the actin cytoskeleton is organized for macropinocytosis by a signalling patch of PIP3 and active Ras and Rac, together with their regulatory proteins and effectors, including the protein kinases Akt and SGK. The Scar/ WAVE complex is recruited to the periphery of this patch, triggering the formation of a hollow ring of protrusive actin polymerization, and eventually a macropinocytic cup. Major problems to be addressed include: the dynamics sustaining macropinocytic patches and the mechanism of Scar/WAVE recruitment; the mechanisms of cup closure and of membrane fusion; the ecological situations where amoebae feed by macropinocytosis; and the evolutionary relationship between macropinocytosis and growth factor signalling.

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Macropinosome formation by tent pole ruffling in macrophages

Cited by 97 publications

References 45 publications

FcRn mediates fast recycling of endocytosed albumin and IgG from early macropinosomes in primary macrophages

FcRn mediates fast recycling of endocytosed albumin and IgG from early macropinosomes in primary macrophages

Rab10 regulates tubular endosome formation through KIF13A/B motors

Living on soup: macropinocytic feeding in amoebae

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