SNX15 links clathrin endocytosis to the PtdIns(3)P early endosome independent of the APPL1 endosome

Danson, Chris M.; Brown, E. G.; Hemmings, Oliver J; McGough, Ian J.; Yarwood, Sam; Heesom, Kate J; Carlton, Jeremy G.; Martín-Serrano, Juan; May, Margaret T; Verkade, Paul; Cullen, Peter J.

doi:10.1242/jcs.125732

Cited by 26 publications

(48 citation statements)

References 49 publications

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“…Remarkably, PI(3)P-binding SNXs implicated in endosomal sorting and with known localization to early and recycling endosomes, such as SNX1, SNX3, SNX4, SNX8, SNX17 and SNX27, accumulated on TfR clusters in MTM1-depleted cells (Figure 18a, b). In contrast, TfR-cluster were negative for SNX15 (Figure 18a, b), which was previously implicated in earlier sorting events such as the progression of CCVs to PI(3)P-enriched early endosomes (Danson, Brown et al 2013). Many SNXs contain BAR domains with membrane deforming activities (Carlton, Bujny et al 2004), some of which we found enriched on TfR-containing endosomes upon MTM1 depletion.…”

Section: Sub-plasma Membrane Early and Recycling Endosomes Accumulatementioning

confidence: 76%

A phosphoinositide conversion mechanism for exit from endosomes

Ketel¹,

Krauß²,

Nicot³

et al. 2016

Nature

165

177

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I owe special thanks to Marnix Wieffer and Michael Krauß, who spent a lot of time helping me to get started in the lab, to overcome numerous experimental problem, I was not sure how to deal with, and frequently joined in discussions about my project with excellent advice. I am really grateful for your experimental support, Michael, and the time you invested in the project during our paper revision.Further, I would like to thank Jocelyn Laporte and his group, especially Anne-Sophie Nicot, at the IGBMC in Strasbourg for their support and a very fruitful collaboration, and Carsten Schultz and his group at the EMBL in Heidelberg for their support and constant supply with PIP/AMs. I owe special thanks to Dmytro Puchkov for the ultrastructural analysis and Eberhard Krause for mass spectrometry done within this project. I also need to acknowledge Markus Wenk and Federico Torta at the Singapore Lipidomics Incubator for joining the project at a very late stage, when we urgently needed help from lipidomics specialists. It was a pity that experiments did not work out as planned.I would further like to express my gratitude to two very skilled technicians in the AG Haucke lab: Silke Zillmann and Delia Löwe. Without your help it would have been impossible to achieve so much within the limited amount of time I had during the paper revision. by VPS34-IN1 treatment................................................... 52 2.3.11 Fluorescence microscopy................................................................................. 53 2.3.12 Flow cytometry............................................................................................ III SummaryPhosphoinositides (PIs) are a minor class of short-lived phospholipids that serve as crucial signposts of membrane identity. Thereby, PIs full fill important functions in cell signaling and membrane transport. PI 4-phosphates such as phosphatitylinositol-4-phosphate (PI(4)P) and phosphatitylinositol-4,5-bisphosphate (PI(4,5)P 2 ) are enriched at the plasma membrane (PM), on secretory organelles and lysosomes, while PI 3-phosphates, i.e.phosphatitylinositol-3-phosphate (PI(3)P), are a hallmark of the endosomal system.Directional transport between these compartments, thus, requires regulated PI conversion.However, PI conversion in exit from PI(3)P-enriched endosomes en route to the PI(4)P-and PI(4,5)P 2 -positive PM in endosomal recycling remained unknown.Here, we report that cargo exit from endosomes requires removal of PI(3)P by the PI(3)P 3-phosphatase myotubularin 1 (MTM1), and concomitant PI(4)P synthesis by PI 4-kinase type II α (PI4K2α). Loss of MTM1 causes endosomal accumulation of PI(3)P and PI(3)P effector proteins, i.e. sorting nexins, Kif16b-mediated outward traffic of PI(3)P containing endosomes and sub-plasmalemmal accumulation of exocytosis-deficient endosomes. As PI4K2α associates with MTM1 and thereby facilitates membrane recruitment of MTM1, these phenotypic changes are mimicked by loss of PI4K2α. The conversion of PI(3)P-to-PI(4)P is paralleled by a switch i...

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Section: Sub-plasma Membrane Early and Recycling Endosomes Accumulatementioning

confidence: 76%

A phosphoinositide conversion mechanism for exit from endosomes

Ketel¹,

Krauß²,

Nicot³

et al. 2016

Nature

165

177

View full text Add to dashboard Cite

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“…Each component of this complex has been shown to promote the lysosomal trafficking and degradation of EGFR (Cavet et al, 2008;Chin et al, 2001;Danson et al, 2013;Gullapalli et al, 2004), but this role appears to be independent of their functions within the retromer (Sun et al, 2013a,b); as of yet, it is not clear whether all four SNX proteins function as a complex to regulate EGFR trafficking. SNX5 contains a PX domain and a Bin-amphiphysinRvs (BAR) domain, and its PX domain specifically binds PtdIns(4,5)P 2 (Koharudin et al, 2009).…”

Section: Intracellular Ptdins(45)p 2 Signalingmentioning

confidence: 99%

Emerging roles of PtdIns(4,5)P2 – beyond the plasma membrane

Tan

Thapa

Choi

et al. 2015

Journal of Cell Science

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Phosphoinositides are a collection of lipid messengers that regulate most subcellular processes. Amongst the seven phosphoinositide species, the roles for phosphatidylinositol 4,5-bisphosphate [PtdIns (4,5)P 2 ] at the plasma membrane, such as in endocytosis, exocytosis, actin polymerization and focal adhesion assembly, have been extensively studied. Recent studies have argued for the existence of PtdIns(4,5)P 2 at multiple intracellular compartments, including the nucleus, endosomes, lysosomes, autolysosomes, autophagic precursor membranes, ER, mitochondria and the Golgi complex. Although the generation, regulation and functions of PtdIns(4,5)P 2 are less well-defined in most other intracellular compartments, accumulating evidence demonstrates crucial roles for PtdIns(4,5)P 2 in endolysosomal trafficking, endosomal recycling, as well as autophagosomal pathways, which are the focus of this Commentary. We summarize and discuss how phosphatidylinositol phosphate kinases, PtdIns(4,5)P 2 and PtdIns(4,5)P 2 -effectors regulate these intracellular protein and membrane trafficking events.

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“…However, SNX20 knock-out mice showed no overt phenotypes related to endothelial cell adhesion, and therefore its precise function is still not clear. Down-regulation of SNX21 by siRNA also has a modest effect on the endocytic degradation of the epidermal growth factor receptor (17), further suggesting a role for these proteins in endosomal transport, although the mechanism underlying this effect has also not been characterized in detail.…”

Section: The Atomic Coordinates and Structure Factors (Code 4ymr) Havmentioning

confidence: 99%

Structure and Membrane Binding Properties of the Endosomal Tetratricopeptide Repeat (TPR) Domain-containing Sorting Nexins SNX20 and SNX21

Clairfeuille

Norwood²,

Qi³

et al. 2015

Journal of Biological Chemistry

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Background: SNX-PXB proteins SNX20 and SNX21 are poorly characterized members of the sorting nexin (SNX) family. Results: We find the SNX-PXB proteins are localized to endosomes, and that the PXB domain has a tetratricopeptide repeat (TPR)-fold. Conclusion:The PXB domain has an atypical TPR-fold with conserved surfaces likely to mediate protein-protein interactions. Significance: SNX-PXB proteins are endosome-associated scaffolds that mediate membrane and protein interactions.

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SNX15 links clathrin endocytosis to the PtdIns(3)P early endosome independent of the APPL1 endosome

Cited by 26 publications

References 49 publications

A phosphoinositide conversion mechanism for exit from endosomes

A phosphoinositide conversion mechanism for exit from endosomes

Emerging roles of PtdIns(4,5)P2 – beyond the plasma membrane

Structure and Membrane Binding Properties of the Endosomal Tetratricopeptide Repeat (TPR) Domain-containing Sorting Nexins SNX20 and SNX21

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