ER-shaping proteins facilitate lipid exchange between the ER and mitochondria in S. cerevisiae
about
A conserved endoplasmic reticulum membrane protein complex (EMC) facilitates phospholipid transfer from the ER to mitochondriaProtrudin binds atlastins and endoplasmic reticulum-shaping proteins and regulates network formationMembrane-shaping disorders: a common pathway in axon degenerationPhospholipid transport via mitochondriaMitochondrial form and functionMembrane contact sites, gateways for lipid homeostasisDynamic formation of ER-PM junctions presents a lipid phosphatase to regulate phosphoinositidesPeroxins Pex30 and Pex29 Dynamically Associate with Reticulons to Regulate Peroxisome Biogenesis from the Endoplasmic ReticulumER-associated mitochondrial division links the distribution of mitochondria and mitochondrial DNA in yeast.Sar1, a Novel Regulator of ER-Mitochondrial Contact Sites.Origin of the Autophagosomal Membrane in PlantsA phospholipid transfer function of ER-mitochondria encounter structure revealed in vitroThe topology and regulation of cardiolipin biosynthesis and remodeling in yeastMitochondrial lipids in neurodegenerationSeparating mitochondrial protein assembly and endoplasmic reticulum tethering by selective coupling of Mdm10Phosphatidylserine synthesis at membrane contact sites promotes its transport out of the ER.Bridging the gap: membrane contact sites in signaling, metabolism, and organelle dynamics.Structure 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.An inside-out origin for the eukaryotic cell.Prolonged starvation drives reversible sequestration of lipid biosynthetic enzymes and organelle reorganization in Saccharomyces cerevisiaeRapid, optimized interactomic screeningConserved SMP domains of the ERMES complex bind phospholipids and mediate tether assemblyPhosphatidylethanolamine Metabolism in Health and Disease.Inositol lipid regulation of lipid transfer in specialized membrane domains.Inheritance of the fittest mitochondria in yeast.A family of membrane-shaping proteins at ER subdomains regulates pre-peroxisomal vesicle biogenesis.Morphology and function of membrane-bound organelles.Transport of phosphatidylserine from the endoplasmic reticulum to the site of phosphatidylserine decarboxylase2 in yeast.Role of membrane contact sites in protein import into mitochondria.Membrane Contact Sites: Complex Zones for Membrane Association and Lipid Exchange.Ascorbate peroxidase proximity labeling coupled with biochemical fractionation identifies promoters of endoplasmic reticulum-mitochondrial contacts.Structure-function insights into direct lipid transfer between membranes by Mmm1-Mdm12 of ERMES.A novel fluorescent reporter detects plastic remodeling of mitochondria-ER contact sites.Perspective on architecture and assembly of membrane contact sites.The ancient and widespread nature of the ER-mitochondria encounter structure.Role of Intra- and Inter-mitochondrial Membrane Contact Sites in Yeast Phospholipid Biogenesis.Mitochondrial Tethers and Their Impact on Lifespan in Budding Yeast.Morphological Pathways of Mitochondrial Division.Identification of multi-copy suppressors for endoplasmic reticulum-mitochondria tethering proteins in Saccharomyces cerevisiae.
P2860
Q21145703-55504728-20AA-4C60-A60C-C8BDAB0B6D23Q24318948-7E72C728-7B38-49A9-ADE3-07D8C03A2A0EQ26852808-04EEE93D-F65D-4CB2-8573-3AC22A6E9B43Q26864864-8ADCA464-8B40-401E-B60F-19B2B9C6B9A6Q26866448-027EA932-9817-4A36-83E5-C2FDACDA51A9Q26999991-4772CE0B-8695-4E8B-86BC-11983061026FQ27309000-B9F57DCC-EDDC-4A18-BC29-2CC42AB72BB5Q27929790-BCDD4EF7-6252-4892-8871-798E296E551CQ27935426-10C28D88-8A67-4C66-9B7B-FDDF85CDAD5EQ27939376-781DEED2-6C22-42E2-9789-CDE1A4D9A09EQ28067655-01747B78-6556-41BC-8058-0AAE83D2519BQ28114335-D03AC237-45F2-4EB7-858A-364365308349Q28397368-0DBC3849-DA00-4AFA-AF4A-10D95EBB2333Q28397548-8103A885-6859-46D4-8C63-B0DCB4273E2BQ30152716-D247C5DE-836C-4E8E-B261-AFFA71AD5D73Q30274928-35BFCE2C-16F2-4D57-A134-FCF738642874Q33797013-5E106559-3431-4ABC-9E23-70F01BF45740Q34503783-5E6E94E9-8A9A-45BF-A6E7-E8997F69E780Q35307797-30C12EB2-28F7-45D2-9DF1-2DA96316568EQ35372352-4360BE24-C799-4ABD-A359-DFCBE7129D02Q35621799-406AE801-FFE4-4A91-8442-EF3782055784Q35665985-B0CED9A0-9AEA-4E81-BD0E-6C30388DBBE4Q35796082-99FA1613-DC87-496A-8BD0-014EDB4063C4Q36652965-D081C8D0-86CA-4A50-8205-21B444230268Q36881382-CFC6F22E-1706-4D37-B0C9-E8B474686090Q37423474-DE89A72E-33F0-4AF4-8001-6CA80F5D2B57Q37429816-D532E0D3-4B76-4A3D-B41E-932667991872Q38188145-FF638A57-A197-4207-B686-C3832CF6DD0EQ38263794-A8BB4178-D931-472B-BD85-7CD38E0D7448Q38290676-D30F38DC-C354-41AB-9076-081486FA7AA4Q38698580-FD5E75DB-C98F-48E4-BFF6-69C19BE8EA95Q42285856-9C62F143-0338-4D9C-842F-5D43A5CF8154Q47253239-661350BA-DED7-4530-A7B4-A754616069F2Q47381756-2E45B61E-B461-4A2B-B69B-8DA15375C998Q47727433-78E01B06-C7A1-4F27-8567-578994D54BFDQ47743514-DAB18551-DCC2-47A2-AE5F-1E7D650CBF82Q47943012-EEECF18F-2B47-403C-813E-31070F116E53Q49480236-0BD526F1-E4B6-465D-9677-4C7D5CC5595CQ49805907-5A802B97-C20A-4E91-8E6C-5D78EC28BBE0Q51567682-AF4B62B1-5033-4FAF-B3A7-F781934E132E
P2860
ER-shaping proteins facilitate lipid exchange between the ER and mitochondria in S. cerevisiae
description
2012 nî lūn-bûn
@nan
2012 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի հուլիսին 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
ER-shaping proteins facilitate ...... mitochondria in S. cerevisiae
@ast
ER-shaping proteins facilitate ...... mitochondria in S. cerevisiae
@en
type
label
ER-shaping proteins facilitate ...... mitochondria in S. cerevisiae
@ast
ER-shaping proteins facilitate ...... mitochondria in S. cerevisiae
@en
prefLabel
ER-shaping proteins facilitate ...... mitochondria in S. cerevisiae
@ast
ER-shaping proteins facilitate ...... mitochondria in S. cerevisiae
@en
P2093
P2860
P356
P1476
ER-shaping proteins facilitate ...... mitochondria in S. cerevisiae
@en
P2093
Barry P Young
Christiane Voss
Christopher J Loewen
Sujoy Lahiri
William A Prinz
P2860
P304
P356
10.1242/JCS.105635
P407
P577
2012-07-13T00:00:00Z