The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex
about
Proteins involved in the degradation of cytoplasmic mRNA in the major eukaryotic model systemsRGG motif proteins: modulators of mRNA functional statesStructural analysis of the yeast Dhh1-Pat1 complex reveals how Dhh1 engages Pat1, Edc3 and RNA in mutually exclusive interactionsActive Site Conformational Dynamics Are Coupled to Catalysis in the mRNA Decapping Enzyme Dcp2A direct interaction between DCP1 and XRN1 couples mRNA decapping to 5' exonucleolytic degradationThe C-Terminal Domain from S. cerevisiae Pat1 Displays Two Conserved Regions Involved in Decapping Factor RecruitmentIn Vitro Reconstitution of a Cellular Phase-Transition Process that Involves the mRNA Decapping MachineryStructure of the Dcp2-Dcp1 mRNA-decapping complex in the activated conformationStructure of the active form of Dcp1-Dcp2 decapping enzyme bound to m7GDP and its Edc3 activatorStructural basis of mRNA-cap recognition by Dcp1-Dcp2Yeast Edc3 targets RPS28B mRNA for decapping by binding to a 3' untranslated region decay-inducing regulatory element.Identification of the Rps28 binding motif from yeast Edc3 involved in the autoregulatory feedback loop controlling RPS28B mRNA decayPhase separation in biology; functional organization of a higher orderATPase activity of the DEAD-box protein Dhh1 controls processing body formationEvidence of conformational selection driving the formation of ligand binding sites in protein-protein interfacesPIWI Slicing and EXD1 Drive Biogenesis of Nuclear piRNAs from Cytosolic Targets of the Mouse piRNA PathwayEdc3 function in yeast and mammals is modulated by interaction with NAD-related compoundsSCD6 induces ribonucleoprotein granule formation in trypanosomes in a translation-independent manner, regulated by its Lsm and RGG domains.Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme.The BEACH Domain Protein SPIRRIG Is Essential for Arabidopsis Salt Stress Tolerance and Functions as a Regulator of Transcript Stabilization and LocalizationPdc1 functions in the assembly of P bodies in Schizosaccharomyces pombe.Competition between Decapping Complex Formation and Ubiquitin-Mediated Proteasomal Degradation Controls Human Dcp2 Decapping Activity.Two-headed tetraphosphate cap analogs are inhibitors of the Dcp1/2 RNA decapping complex.Control of mRNA decapping by positive and negative regulatory elements in the Dcp2 C-terminal domainAnalysis of the Physiological Activities of Scd6 through Its Interaction with Hmt1P-bodies and stress granules: possible roles in the control of translation and mRNA degradation.Spatial control of translation repression and polarized growth by conserved NDR kinase Orb6 and RNA-binding protein Sts5Structural and functional control of the eukaryotic mRNA decapping machinery.Argonaute and GW182 proteins: an effective alliance in gene silencing.The role of disordered protein regions in the assembly of decapping complexes and RNP granules.A synergistic network of interactions promotes the formation of in vitro processing bodies and protects mRNA against decapping.Addressing recent docking challenges: A hybrid strategy to integrate template-based and free protein-protein docking.Protein-protein and peptide-protein docking and refinement using ATTRACT in CAPRI.Modeling oblong proteins and water-mediated interfaces with RosettaDock in CAPRI rounds 28-35.The S. pombe mRNA decapping complex recruits cofactors and an Edc1-like activator through a single dynamic surface.A general method for rapid and cost-efficient large-scale production of 5' capped RNA.The decapping activator Edc3 and the Q/N-rich domain of Lsm4 function together to enhance mRNA stability and alter mRNA decay pathway dependence in Saccharomyces cerevisiae.The Lsm1-7-Pat1 complex promotes viral RNA translation and replication by differential mechanisms.Arginine methylation promotes translation repression activity of eIF4G-binding protein, Scd6.A unique surface on Pat1 C-terminal domain directly interacts with Dcp2 decapping enzyme and Xrn1 5'-3' mRNA exonuclease in yeast.
P2860
Q26864165-02568769-6691-4535-945B-E6A97AEB00F4Q26998590-2B8B61A4-6BC2-4DD8-A579-E3C94F636AEFQ27679086-6ED3FEC9-6A96-4F47-BD06-AC25ED8E9EF4Q27679348-B046B55E-74FF-403B-84B8-DC29D03F7FFEQ27683382-A734C8EE-A158-49FC-A0F0-C76A9DA558D6Q27683791-08C226DA-FEAF-4DE8-8C58-059524991446Q27683953-B4B414DA-E6EA-4B0E-9133-2E57971AC5F6Q27704871-A52115E5-C9A4-4C05-BCF2-55D4791F3871Q27728161-F7688D35-C961-4392-B0BA-7097D507EC54Q27728162-C91E86F2-3F30-4212-956D-A379531195C8Q27930271-16CAC731-695D-40A5-9BFF-C5FFF92DA7E5Q27935536-B4FF2586-730A-4887-A036-CCD3E988FDECQ28071484-071C8D95-6856-4404-92A7-B57B12DEF578Q28114329-27FF5D0D-B587-4879-BE64-9B7F1BAB32DCQ28543479-3EFFEF49-F18D-4D17-8223-DC0C63E9DEE5Q28592070-AC095520-3A63-48B0-BBFA-986F3BA2F577Q30412475-13DB6534-F183-43A6-8390-2366DB75B58AQ30540960-7FC09752-4A74-4D63-8560-67785DC59B42Q33790825-D80E5E73-5013-4CD0-9EFF-14335CD8537EQ34483167-8C48C6F5-DF14-4B97-95A2-B1B0644C5F7AQ34547906-31D84F38-40E8-4599-A457-5CE4D3F20F8CQ35626088-53092332-E6AF-43AC-A3F4-B198C248B9BAQ35908793-07603241-520A-4DEA-AA7E-A9614E8CBFE2Q35952788-F10F014C-3AB8-4912-A5CD-416914604CAEQ36173018-EDB58D1A-E8C1-45DF-8834-F8D63008B48DQ36192936-9C2FBD97-5772-4960-8832-73660A19F5F9Q37232254-0BA07A64-7AF2-449B-A215-FFD44A984657Q38071446-C4C49751-4E81-4DF0-A7EB-1F5ADE8BAAAAQ38122217-22604E9C-4DF1-4277-9A28-36237029DAAEQ38172402-8B99F134-080F-43BC-A30B-16A0DDC9692FQ38803933-0581E894-C44B-40C5-BCF1-B09A63139CC8Q39062782-33248D85-E389-4650-8E3F-DB6939BC69A7Q39245081-A24BFC6B-7D4F-4671-8BE4-8472664067FCQ39352554-6F572AF6-B659-4BF8-B6A9-88198C8F2E58Q39646789-F95F42D8-2C27-4C93-BA57-69418164262CQ40671228-6E72BC0B-2775-4F8D-9863-E13B2BFEAD33Q41627669-EC05631F-591D-4DD6-A132-678F8D7CC9DEQ41655623-11B8EE7C-5237-493E-85BE-799EEF45DE53Q42111476-FF8A173A-92A2-41B0-9F16-1DA16BD73C5CQ46273140-EBA63E1C-ACEA-4FDE-9B02-581A1C93EBB1
P2860
The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex
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
The structural basis of Edc3- ...... p1:Dcp2 mRNA decapping complex
@ast
The structural basis of Edc3- ...... p1:Dcp2 mRNA decapping complex
@en
The structural basis of Edc3- ...... p1:Dcp2 mRNA decapping complex
@nl
type
label
The structural basis of Edc3- ...... p1:Dcp2 mRNA decapping complex
@ast
The structural basis of Edc3- ...... p1:Dcp2 mRNA decapping complex
@en
The structural basis of Edc3- ...... p1:Dcp2 mRNA decapping complex
@nl
prefLabel
The structural basis of Edc3- ...... p1:Dcp2 mRNA decapping complex
@ast
The structural basis of Edc3- ...... p1:Dcp2 mRNA decapping complex
@en
The structural basis of Edc3- ...... p1:Dcp2 mRNA decapping complex
@nl
P2860
P50
P3181
P356
P1433
P1476
The structural basis of Edc3- ...... p1:Dcp2 mRNA decapping complex
@en
P2093
Julia Kamenz
Remco Sprangers
P2860
P304
P3181
P356
10.1038/EMBOJ.2011.408
P407
P577
2012-01-18T00:00:00Z