Membrane recognition by phospholipid-binding domains

Lemmon, Mark A.

doi:10.1038/nrm2328

Cited by 1,311 publications

(1,546 citation statements)

References 116 publications

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“…Annexins have long been considered as potential regulators of cholesterol-rich membrane microdomains at the PM (Gerke et al , 2005; Lemmon, 2008; Grewal et al , 2010; Enrich et al , 2011). This was considered to occur mainly via annexins interacting directly with other regulatory proteins or lipids, thereby creating and stabilizing membrane microenvironments.…”

Section: Discussionmentioning

confidence: 99%

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Cholesterol transport from late endosomes to the Golgi regulates t-SNARE trafficking, assembly, and function

Reverter¹,

Rentero²,

Muga³

et al. 2011

Molecular Biology of the Cell

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This study shows that impaired cholesterol egress from late endosomes in cells with high annexin A6 levels is associated with altered soluble N-ethylmaleimide–sensitive fusion protein 23 (SNAP23) and syntaxin-4 cellular distribution and assembly and accumulation in Golgi membranes. This correlates with reduced secretion of cargo along the constitutive and SNAP23/syntaxin-4–dependent secretory pathway.

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Section: Discussionmentioning

confidence: 99%

“…In recent years, the involvement of annexins in membrane recognition and trafficking has emerged as one of their predominant functions (Gerke and Moss, 2002; Gerke et al , 2005; Lemmon, 2008; Grewal et al , 2010; Enrich et al , 2011). Annexins are a family of structurally related Ca 2+ -regulated membrane-binding proteins.…”

Section: Introductionmentioning

confidence: 99%

Cholesterol transport from late endosomes to the Golgi regulates t-SNARE trafficking, assembly, and function

Reverter¹,

Rentero²,

Muga³

et al. 2011

Molecular Biology of the Cell

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“…phosphatidylserine (PS) are more abundant with 8.5% of total lipids (Wenk, Lucast et al 2003;Lemmon 2008). This emphasizes the fundamental importance and regulatory role of PIs in processes such as membrane trafficking and signaling,…”

Section: Phosphoinositides Determine Membrane Identitymentioning

confidence: 99%

“…Membrane recruitment of PI effector proteins is mediated via PI binding domains (Lemmon 2008). 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.…”

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%

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A phosphoinositide conversion mechanism for exit from endosomes

Ketel¹,

Krauß²,

Nicot³

et al. 2016

Nature

157

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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Quantitative Analysis of Phosphoinositide 3‐Kinase (PI3K) Signaling Using Live‐Cell Total Internal Reflection Fluorescence (TIRF) Microscopy

Johnson

Haugh

2013

CP Cell Biology

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This unit focuses on the use of total internal reflection fluorescence (TIRF) microscopy and image analysis methods to study the dynamics of signal transduction mediated by class I phosphoinositide 3‐kinases (PI3Ks) in mammalian cells. The first four protocols cover live‐cell imaging experiments, image acquisition parameters, and basic image processing and segmentation. These methods are generally applicable to live‐cell TIRF experiments. The remaining protocols outline more advanced image analysis methods, which were developed in our laboratory for the purpose of characterizing the spatiotemporal dynamics of PI3K signaling. These methods may be extended to analyze other cellular processes monitored using fluorescent biosensors. Curr. Protoc. Cell Biol. 61:14.14.1‐14.14.24. © 2013 by John Wiley & Sons, Inc.

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Membrane recognition by phospholipid-binding domains

Cited by 1,311 publications

References 116 publications

Cholesterol transport from late endosomes to the Golgi regulates t-SNARE trafficking, assembly, and function

Cholesterol transport from late endosomes to the Golgi regulates t-SNARE trafficking, assembly, and function

A phosphoinositide conversion mechanism for exit from endosomes

Quantitative Analysis of Phosphoinositide 3‐Kinase (PI3K) Signaling Using Live‐Cell Total Internal Reflection Fluorescence (TIRF) Microscopy

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