Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer - Wikidata - wikimedia - TriplyDB

Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer

Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer

http://www.wikidata.org/entity/Q24298007

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A conserved endoplasmic reticulum membrane protein complex (EMC) facilitates phospholipid transfer from the ER to mitochondria Extended Synaptotagmin (ESyt) Triple Knock-Out Mice Are Viable and Fertile without Obvious Endoplasmic Reticulum Dysfunction Inter-organelle ER-endolysosomal contact sites in metabolism and disease across evolution Membrane contact sites, gateways for lipid homeostasis Dynamic formation of ER-PM junctions presents a lipid phosphatase to regulate phosphoinositides Induction of stable ER-plasma-membrane junctions by Kv2.1 potassium channels.A new family of StART domain proteins at membrane contact sites has a role in ER-PM sterol transport.Ltc1 is an ER-localized sterol transporter and a component of ER-mitochondria and ER-vacuole contacts.ER-mitochondrial junctions can be bypassed by dominant mutations in the endosomal protein Vps13.Lipid transport by TMEM24 at ER-plasma membrane contacts regulates pulsatile insulin secretion Plant ER geometry and dynamics: biophysical and cytoskeletal control during growth and biotic response.A Systems Biology Approach Using Transcriptomic Data Reveals Genes and Pathways in Porcine Skeletal Muscle Affected by Dietary Lysine The Emerging Network of Mitochondria-Organelle Contacts.Structure and function of ER membrane contact sites with other organelles Extended synaptotagmins (E-Syts): Architecture and dynamics of membrane contact sites revealed.Three-dimensional architecture of extended synaptotagmin-mediated endoplasmic reticulum-plasma membrane contact sites.Lipids under stress--a lipidomic approach for the study of mood disorders.Conserved SMP domains of the ERMES complex bind phospholipids and mediate tether assembly The ER/PM microdomain, PI(4,5)P₂ and the regulation of STIM1-Orai1 channel function.The STIM1-ORAI1 microdomain Identification and characterization of β-sitosterol target proteins.Neurospora crassa transcriptomics reveals oxidative stress and plasma membrane homeostasis biology genes as key targets in response to chitosan.Extended synaptotagmins are Ca2+-dependent lipid transfer proteins at membrane contact sites.Control of plasma membrane lipid homeostasis by the extended synaptotagmins The effects of ER morphology on synaptic structure and function in Drosophila melanogaster.An inducible ER-Golgi tether facilitates ceramide transport to alleviate lipotoxicity Organelle biogenesis and interorganellar connections: Better in contact than in isolation.Role of membrane contact sites in protein import into mitochondria.SMP-domain proteins at membrane contact sites: Structure and function Membrane Contact Sites: Complex Zones for Membrane Association and Lipid Exchange.Advances on the Transfer of Lipids by Lipid Transfer Proteins Homeostatic regulation of the PI(4,5)P2-Ca(2+) signaling system at ER-PM junctions.ER-plasma membrane contact sites contribute to autophagosome biogenesis by regulation of local PI3P synthesis.Crystal structure of Mdm12 and combinatorial reconstitution of Mdm12/Mmm1 ERMES complexes for structural studies.No Evidence for Spontaneous Lipid Transfer at ER-PM Membrane Contact Sites.The coming of age of the mitochondria-ER contact: a matter of thickness.The Extended-Synaptotagmins.Mitochondria-organelle contact sites: the plot thickens.ER-plasma membrane junctions: Why and how do we study them?Tubular lipid binding proteins (TULIPs) growing everywhere.

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P2860

Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer

http://www.wikidata.org/entity/Q24298007

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2014 nî lūn-bûn

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2014 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2014 թվականի հունիսին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer

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Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer

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Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer

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Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer

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Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer

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Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer

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Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer

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Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer

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Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer

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Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer

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Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer

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Curtis M Schauder

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Karin M Reinisch

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Markus R Wenk

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Pradeep Narayanaswamy

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Xudong Wu

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P2860

PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by the extended synaptotagmins.

E-Syts, a family of membranous Ca2+-sensor proteins with multiple C2 domains

Structure and Ca²⁺-binding properties of the tandem C₂ domains of E-Syt2

An ER-mitochondria tethering complex revealed by a synthetic biology screen

Osh4p exchanges sterols for phosphatidylinositol 4-phosphate between lipid bilayers

Membrane lipids: where they are and how they behave

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Crystal structure of cholesteryl ester transfer protein reveals a long tunnel and four bound lipid molecules

Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution

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10.1038/NATURE13269

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7506

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510

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Pietro De Camilli

Yasunori Saheki

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2014-06-26T00:00:00Z

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identical protein binding

Extended synaptotagmin 2

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