Organelle identity and the signposts for membrane traffic

Behnia, Rudy; Munro, Sean

doi:10.1038/nature04397

Cited by 457 publications

(448 citation statements)

References 102 publications

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“…Notably, no PI species has been assigned to recycling endosomes so far. Modified from (Behnia and Munro 2005).…”

Section: Exocytic Membrane Transport Is Counterbalanced By Retrogradementioning

confidence: 99%

“…GTPases of the Arf and Rab families (Behnia and Munro 2005). These proteins can regulate localization and/ or enzymatic activity of PI kinases and phosphatases in their GTP-and membrane-bound state, and thus provide spatiotemporal regulation of PI composition and mechanisms for positive and negative feed back loops.…”

Section: Intracellular Membrane Identity Is Further Defined By the Sumentioning

confidence: 99%

“…However, as PI-protein interactions are of moderate affinity, efficient recruitment often requires coincidence detection of a specific small GTPase, PIs (Di Paolo and De Camilli 2006) and in some cases additional protein-protein interactions, i.e. during clathrin-mediated endocytosis (Godi, Pertile et al 1999;Behnia and Munro 2005;Lemmon 2008). This fundamental concept applies to transport carrier biogenesis at various subcellular compartments, despite the diversity of coat proteins (Santiago-Tirado and Bretscher 2011).…”

Section: Intracellular Membrane Identity Is Further Defined By the Sumentioning

confidence: 99%

“…Small GTPases, including members of the Rab family are ideally suited to discriminate between endosomal subpopulations as -together with different PI species -they serve as spatial landmarks conferring membrane identity (Behnia and Munro 2005).…”

Section: Sub-plasma Membrane Early and Recycling Endosomes Accumulatementioning

confidence: 99%

“…Directional membrane trafficking frequently conincides with a switch in endosomal PI-as well as Rab-identity (Behnia and Munro 2005). To address the Rab-identity of exocytic vesicles we applied dual-color TIRF microscopy to monitor Tf exocytosis in cells expressing GFP-tagged variants of different Rab proteins.…”

Section: Rab11 Is Required For Endosomal Exocyst Localizationmentioning

confidence: 99%

See 4 more Smart Citations

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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“…Notably, no PI species has been assigned to recycling endosomes so far. Modified from (Behnia and Munro 2005).…”

Section: Exocytic Membrane Transport Is Counterbalanced By Retrogradementioning

confidence: 99%

Section: Intracellular Membrane Identity Is Further Defined By the Sumentioning

confidence: 99%

Section: Intracellular Membrane Identity Is Further Defined By the Sumentioning

confidence: 99%

Section: Sub-plasma Membrane Early and Recycling Endosomes Accumulatementioning

confidence: 99%

Section: Rab11 Is Required For Endosomal Exocyst Localizationmentioning

confidence: 99%

See 3 more Smart Citations

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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In vitro reconstitution of small GTPase regulation

et al. 2022

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Small GTPases play essential roles in the organization of eukaryotic cells. In recent years, it has become clear that their intracellular functions result from intricate biochemical networks of the GTPase and their regulators that dynamically bind to a membrane surface. Due to the inherent complexities of their interactions, however, revealing the underlying mechanisms of action is often difficult to achieve from in vivo studies. This review summarizes in vitro reconstitution approaches developed to obtain a better mechanistic understanding of how small GTPase activities are regulated in space and time.

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The TRAPP complexes: oligomeric exchange factors that activate the small GTPases Rab1 and Rab11

Galindo

Munro

2022

FEBS Letters

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The Transport Protein Particle (TRAPP) complexes are highly conserved multisubunit complexes that act as nucleotide exchange factors (GEFs) for Rab GTPases. They act in both protein secretion and autophagy and have also been proposed to have a role in other processes such as cytokinesis and ciliogenesis. There are two TRAPP complexes in metazoans: TRAPPII, which activates Rab11; and TRAPPIII, which activates Rab1. Both complexes share a core of small subunits that form the active site for the exchange of GDP for GTP. In addition, each TRAPP complex has distinct large subunits that determine the specificity of each complex towards its substrate Rab and are essential for activity in vivo. Crystal structures have revealed the organisation of the TRAPP core and the mechanism of Rab1 activation, whilst recent cryo‐EM structures have unveiled the arrangement of the specific subunits around the core to form each complex. Combining these findings with functional experiments has allowed the proposal of mechanisms for how the specificity of each complex towards their cognate Rab is determined and for the arrangement of these large complexes on the membrane.

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Organelle identity and the signposts for membrane traffic

Cited by 457 publications

References 102 publications

A phosphoinositide conversion mechanism for exit from endosomes

A phosphoinositide conversion mechanism for exit from endosomes

In vitro reconstitution of small GTPase regulation

The TRAPP complexes: oligomeric exchange factors that activate the small GTPases Rab1 and Rab11

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