Sorting nexin 8 regulates endosome-to-Golgi transport

Dyve, Anne Berit; Bergan, Jonas; Utskarpen, Audrun; Sandvig, Kirsten

doi:10.1016/j.bbrc.2009.09.076

Cited by 71 publications

(64 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…S2 and S3). This association is consistent with proposed roles for both SNX8 and SNX3 in endosome to Golgi recycling pathways (8,41,42), but like the SNX8-SNX6 complex will require further validation in vivo to confirm its functional importance.…”

Section: Discussionsupporting

confidence: 67%

Rapid Mapping of Interactions between Human SNX-BAR Proteins Measured In Vitro by AlphaScreen and Single-molecule Spectroscopy

Sierecki

Stevers

Giles

et al. 2014

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

Protein dimerization and oligomerization is commonly used by nature to increase the structural and functional complexity of proteins. Regulated protein assembly is essential to transfer information in signaling, transcriptional, and membrane trafficking events. Here we show that a combination of cell-free protein expression, a proximity based interaction assay (AlphaScreen), and single-molecule fluorescence allow rapid mapping of homo-and hetero-oligomerization of proteins. We have applied this approach to the family of BAR domain-containing sorting nexin (SNX-BAR) proteins, which are essential regulators of membrane trafficking and remodeling in all eukaryotes. Dimerization of BAR domains is essential for creating a concave structure capable of sensing and inducing membrane curvature. We have systematically mapped 144 pairwise interactions between the human SNX-BAR proteins and generated an interaction matrix of preferred dimerization partners for each family member. We find that while nine SNX-BAR proteins are able to form homo-dimers, several including the retromer-associated SNX1, SNX2, and SNX5 require heteromeric interactions for dimerization. SNX2, SNX4, SNX6, and SNX8 show a promiscuous ability to bind other SNX-BAR proteins and we also observe a novel interaction with the SNX3 protein which lacks the BAR domain structure. Molecular & Cellular Proteomics

show abstract

Section: Discussionsupporting

confidence: 67%

Rapid Mapping of Interactions between Human SNX-BAR Proteins Measured In Vitro by AlphaScreen and Single-molecule Spectroscopy

Sierecki

Stevers

Giles

et al. 2014

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

show abstract

“…For example, SNX8 localizes to EE and partially co-localizes with the retromer complex, its suppression has a direct effect on the retrograde transport endosome-to-TGN trafficking [45], but little is known about the biology and biochemistry of this protein [36]. Whether SNX8 couples to motor proteins remains to be seen.…”

Section: Co-ordination Of Endosomal Sorting and Motor Proteinsmentioning

confidence: 98%

The role of motor proteins in endosomal sorting

Hunt

Stephens

2011

Biochemical Society Transactions

View full text Add to dashboard Cite

Microtubule motor proteins play key roles in the spatial organization of intracellular organelles as well as the transfer of material between them. This is well illustrated both by the vectorial transfer of biosynthetic cargo from the endoplasmic reticulum to the Golgi apparatus as well as the sorting of secretory and endocytic cargo in the endosomal system. Roles have been described for dynein and kinesin motors in each of these steps. Cytoplasmic dynein is a highly complex motor comprising multiple subunits that provide functional specialization. The family of human kinesins includes over 40 members. This complexity provides immense functional diversity, yet little is known of the specific requirements and functions of individual motors during discrete membrane trafficking steps. In the present paper, we describe some of the latest findings in this area that seek to define the mechanisms of recruitment and control of activity of microtubule motors in spatial organization and cargo trafficking through the endosomal network.

show abstract

“…PI(3)Pdependent endosomal sorting via SNXs includes: SNX27-retromer mediated recycling of PDZ-ligand-containing cargo proteins (Temkin, Lauffer et al 2011); The SNX1/2/5/6-retromer-mediated or SNX8-mediated endosome-to-TGN trafficking (Dyve, Bergan et al 2009); SNX4-or SNX 17-mediated recycling of TfR (Traer, Rutherford et al 2007) and β1-integrin (Steinberg, Heesom et al 2012), respectively. Since muscle fibers from XLCNMpatients display endosomal accumulation of β1-integrins, we addressed its endosomal sorting and exocytic transport.…”

Section: Figure 3: Tubular Cargo-enriched Subdomains At the Early Sormentioning

confidence: 99%

A phosphoinositide conversion mechanism for exit from endosomes

Ketel¹,

Krauß²,

Nicot³

et al. 2016

Nature

161

177

View full text Add to dashboard Cite

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...

show abstract

Sorting nexin 8 regulates endosome-to-Golgi transport

Cited by 71 publications

References 34 publications

Rapid Mapping of Interactions between Human SNX-BAR Proteins Measured In Vitro by AlphaScreen and Single-molecule Spectroscopy

Rapid Mapping of Interactions between Human SNX-BAR Proteins Measured In Vitro by AlphaScreen and Single-molecule Spectroscopy

The role of motor proteins in endosomal sorting

A phosphoinositide conversion mechanism for exit from endosomes

Contact Info

Product

Resources

About