A conserved membrane-binding domain targets proteins to organelle contact sites.
about
PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by the extended synaptotagmins.Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transferStructure and Ca²⁺-binding properties of the tandem C₂ domains of E-Syt2Extended Synaptotagmin (ESyt) Triple Knock-Out Mice Are Viable and Fertile without Obvious Endoplasmic Reticulum DysfunctionInter-organelle ER-endolysosomal contact sites in metabolism and disease across evolutionMembrane contact sites, gateways for lipid homeostasisDynamic formation of ER-PM junctions presents a lipid phosphatase to regulate phosphoinositidesA new family of StART domain proteins at membrane contact sites has a role in ER-PM sterol transport.ER-associated mitochondrial division links the distribution of mitochondria and mitochondrial DNA in yeast.Mdm1/Snx13 is a novel ER-endolysosomal interorganelle tethering proteinIst2 in the yeast cortical endoplasmic reticulum promotes trafficking of the amino acid transporter Bap2 to the plasma membrane.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 secretionAnalysis of mutations in Neurospora crassa ERMES components reveals specific functions related to β-barrel protein assembly and maintenance of mitochondrial morphology.Understanding of anesthesia - Why consciousness is essential for life and not based on genes.Bridging the gap: membrane contact sites in signaling, metabolism, and organelle dynamics.ER-PM connections: sites of information transfer and inter-organelle communicationThe Emerging Network of Mitochondria-Organelle Contacts.The yeast sphingolipid signaling landscape.The Arabidopsis synaptotagmin SYTA regulates the cell-to-cell movement of diverse plant virusesStructure and function of ER membrane contact sites with other organellesMiro's N-terminal GTPase domain is required for transport of mitochondria into axons and dendrites.Evolutionary Engineering Improves Tolerance for Replacement Jet Fuels in Saccharomyces cerevisiaeThree-dimensional architecture of extended synaptotagmin-mediated endoplasmic reticulum-plasma membrane contact sites.Conserved SMP domains of the ERMES complex bind phospholipids and mediate tether assemblyThe ER/PM microdomain, PI(4,5)P₂ and the regulation of STIM1-Orai1 channel function.Orai1 and STIM1 in ER/PM junctions: roles in pancreatic cell function and dysfunctionPlasma membrane--endoplasmic reticulum contact sites regulate phosphatidylcholine synthesis.Extended synaptotagmins are Ca2+-dependent lipid transfer proteins at membrane contact sites.Control of plasma membrane lipid homeostasis by the extended synaptotagminsEndoplasmic reticulum-mitochondria contacts: function of the junction.An inducible ER-Golgi tether facilitates ceramide transport to alleviate lipotoxicityQuantitative proteomics reveal proteins enriched in tubular endoplasmic reticulum of Saccharomyces cerevisiaeA close-up view of membrane contact sites between the endoplasmic reticulum and the endolysosomal system: from yeast to man.Morphology and function of membrane-bound organelles.Interorganellar membrane microdomains: dynamic platforms in the control of calcium signaling and apoptosis.SMP-domain proteins at membrane contact sites: Structure and functionMembrane Contact Sites: Complex Zones for Membrane Association and Lipid Exchange.Crystal structure of Mdm12 and combinatorial reconstitution of Mdm12/Mmm1 ERMES complexes for structural studies.
P2860
Q24296452-C2C60156-02FF-4ABA-B320-657C927F75C2Q24298007-58DD48B8-3777-4CE4-B7D6-103F1C565BDEQ24316485-58E06F75-CB90-428D-927D-081F06FF8EA0Q26269815-817275CD-7FD1-4C53-8A92-699CEFBCBDE2Q26739484-0F67FAFB-C556-4FDB-B3C2-9D9DBC9720CEQ26999991-9E560331-78D9-4B93-B462-D67BD065D5FCQ27309000-AFEFB596-079A-49EF-B8E1-CD4215AD2303Q27934991-DF7C1710-4503-427D-9BB6-836EE54CE131Q27935426-7E40FBAB-DB1B-4819-80E3-76248FC7558EQ27935790-7F4277A6-AE15-4FCA-8E3F-5454F15D9E22Q27936456-FEBFE795-2499-4171-AAB0-5EB5E859A274Q27937589-ED57AC9D-CE1B-4D8B-A25A-9DC5D130E453Q27938082-C599175A-C4DB-47ED-9ED3-E4EA45B643CDQ28975771-4EE6FC79-7BAB-41F1-BFB5-1BEC5B32EAEBQ30153533-94A0BEDC-31B5-47EC-BF95-1795BF5D088FQ30396974-74C3E464-32F6-464B-A854-AA22F42B95E0Q33797013-43C951DA-ED01-48F9-A69D-DF3D26D79933Q33819894-B8FF61E5-43FC-4DD9-9DFE-C2C9A7762625Q34046376-16E9E3CE-90F1-4FAF-BCC3-E67BB95B1383Q34414198-2435C199-6728-4811-9256-ABE27E58876FQ34462217-CEAA12A4-7045-4A7F-B310-5E41BBDB09F0Q34503783-3D643852-4028-4717-AA8D-963B8E4EF794Q35307797-A8D2562F-304B-476B-ADF8-DAB715626DAEQ35529883-B5D22F88-2184-484F-B3B5-22331080A85EQ35549214-CCC80ADE-9AD8-4233-8E91-F25E078866B4Q35796082-D01DB43D-B552-46C4-B158-8A10A75F0694Q36042455-F4F1C778-199E-4F9E-8FD0-C52C1934B7A9Q36698782-4E48C6C6-76FE-425F-8D1D-EDD787BD7E24Q36812575-13ACD287-B041-4D35-8FFB-3F812310BBE1Q36831617-B958AD76-D4CD-401D-B7B0-9F4FB88F5101Q36844756-F10FFF37-6F22-48B5-8B62-85B4E011B111Q37417736-DB586481-F306-4AE1-BC66-37CC35A8B9D0Q37576605-BE55F4F5-F4F2-4AEC-9ED0-0CF1FDA6CB7EQ37712225-D5A89624-4CE0-41DC-88FC-24F2005D6351Q38175064-A201684C-F7C5-450D-999F-4A3928505201Q38188145-7686B846-9D46-42B2-9719-3F3CDE034D3FQ38588644-84FE76F6-0E52-4850-AC7B-0F5F382BEA22Q38674315-0C9751FD-3FBD-4F5D-A565-FDBB331E5F37Q38698580-0DD86CE1-1767-41AD-98E7-57AC4B015160Q38799711-57CF495A-3747-41AB-A96D-B062B3CDB25E
P2860
A conserved membrane-binding domain targets proteins to organelle contact sites.
description
2012 nî lūn-bûn
@nan
2012 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
A conserved membrane-binding domain targets proteins to organelle contact sites.
@ast
A conserved membrane-binding domain targets proteins to organelle contact sites.
@en
A conserved membrane-binding domain targets proteins to organelle contact sites.
@nl
type
label
A conserved membrane-binding domain targets proteins to organelle contact sites.
@ast
A conserved membrane-binding domain targets proteins to organelle contact sites.
@en
A conserved membrane-binding domain targets proteins to organelle contact sites.
@nl
prefLabel
A conserved membrane-binding domain targets proteins to organelle contact sites.
@ast
A conserved membrane-binding domain targets proteins to organelle contact sites.
@en
A conserved membrane-binding domain targets proteins to organelle contact sites.
@nl
P2860
P3181
P356
P1476
A conserved membrane-binding domain targets proteins to organelle contact sites.
@en
P2093
Alexandre Toulmay
William A Prinz
P2860
P3181
P356
10.1242/JCS.085118
P407
P577
2012-01-01T00:00:00Z