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Search results 101 to 157 out of 157 for Eef2

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Type Details Score
Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Protein
Q99LT6
Organism: Mus musculus/domesticus
Length: 287  
Fragment?: true
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Protein
Q6P9L9
Organism: Mus musculus/domesticus
Length: 843  
Fragment?: true
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Publication
35176139 | J:326167
First Author: Chen Q
Year: 2022
Journal: Blood
Title: Inhibition of LDHA to induce eEF2 release enhances thrombocytopoiesis.
Volume: 139
Issue: 19
Pages: 2958-2971
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Publication
32499677 | J:310669
 
First Author: David O
Year: 2020
Journal: Front Mol Neurosci
Title: D1 Dopamine Receptor Activation Induces Neuronal eEF2 Pathway-Dependent Protein Synthesis.
Volume: 13
Pages: 67
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Publication
34895463 | J:316407
   
First Author: Knight JR
Year: 2021
Journal: Elife
Title: Rpl24Bst mutation suppresses colorectal cancer by promoting eEF2 phosphorylation via eEF2K.
Volume: 10
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Publication
30667373 | J:270447
First Author: Beckelman BC
Year: 2019
Journal: J Clin Invest
Title: Genetic reduction of eEF2 kinase alleviates pathophysiology in Alzheimer's disease model mice.
Volume: 129
Issue: 2
Pages: 820-833
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Publication
28574509 | J:268301
First Author: Delaidelli A
Year: 2017
Journal: Cell Death Differ
Title: MYCN amplified neuroblastoma requires the mRNA translation regulator eEF2 kinase to adapt to nutrient deprivation.
Volume: 24
Issue: 9
Pages: 1564-1576
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Publication
8641144 | J:33345
First Author: Hayes H
Year: 1996
Journal: Cytogenet Cell Genet
Title: Localization of ZNF164, ZNF146, GGTA1, SOX2, PRLR and EEF2 on homoeologous cattle, sheep and goat chromosomes by fluorescent in situ hybridization and comparison with the human gene map.
Volume: 72
Issue: 4
Pages: 342-6
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Publication
14976550 | -
First Author: Spahn CM
Year: 2004
Journal: EMBO J
Title: Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation.
Volume: 23
Issue: 5
Pages: 1008-19
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DO Term
DOID:0050975 | spinocerebellar ataxia type 26
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GO Term
GO:0004686 | elongation factor-2 kinase activity
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Protein Domain
IPR022847 | Transl_elong_IF5A_arc
Type: Family
Description: Eukaryotic eIF-5A was initially thought to function as a translation initiation factor, based on its ability to stimulate methionyl-puromycin synthesis. However, subsequent work revealed a role for eIF5A in translation elongation [, ]. Depletion or inactivation of eIF-5A in the yeast Saccharomyces cerevisiae (Baker's yeast) resulted in the accumulation of polysomes and an increase in ribosomal transit times. Addition of recombinant eIF-5A from yeast, but not a derivative lacking hypusine, enhanced the rate of tripeptide synthesis in vitro. Moreover, inactivation of eIF-5A mimicked the effects of the eEF2 inhibitor sordarin, indicating that eIF-5A might function together with eEF2 to promote ribosomal translocation. Finally, it was shown that eIF5A is specifically required to promote peptide-bond formation between consecutive proline residues. It has been proposed to stimulate the peptidyl-transferase activity of the ribosome and facilitate the reactivity of poor substrates like proline [].eIF-5A is a cofactor for the Rev and Rex transactivator proteins of human immunodeficiency virus-1 and T-cell leukaemia virus I, respectively [, , ]. IF-5A is the sole protein in eukaryotes and archaea to contain the unusual amino acid hypusine (Ne-(4-amino-2-hydroxybutyl)lysine) that is an absolute functional requirement. The first step in the post-translational modification of lysine to hypusine is catalyzed by the enzyme deoxyhypusine synthase, the structure of which has been reported []. The archaeal IF-5A proteins have not been studied as comprehensively as their eukaryotic homologues, though the crystal structure of the Pyrobaculum aerophilum protein has been determined. Unmodified P. aerophilum IF-5A is found to be a beta structure with two domains and three separate hydrophobic cores. The lysine (Lys42) that is post-translationally modified by deoxyhypusine synthase is found at one end of the IF-5A molecule in a turn between beta strands beta4 and beta5; this lysine residue is freely solvent accessible. The C-terminal domain is found to be homologous to the cold-shock protein CspA of E. coli, which has a well characterised RNA-binding fold, suggesting that IF-5A is involved in RNA binding [].This entry represents the archaeal IF-5A proteins.
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HT Experiment
E-GEOD-80633 | Gene expression analysis in cortex of CRTC1 deficient mice and WT littermates
Series Id: GSE80633
Experiment Type: transcription profiling by array
Study Type: WT vs. Mutant
Source: ArrayExpress
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Publication
34815424 | J:334176
First Author: Smith PR
Year: 2021
Journal: Nat Commun
Title: Functionally distinct roles for eEF2K in the control of ribosome availability and p-body abundance.
Volume: 12
Issue: 1
Pages: 6789
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Publication
24012003 | J:201741
First Author: Um JW
Year: 2013
Journal: Neuron
Title: Metabotropic glutamate receptor 5 is a coreceptor for Alzheimer aβ oligomer bound to cellular prion protein.
Volume: 79
Issue: 5
Pages: 887-902
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Publication
36384136 | J:332627
First Author: Zhou Q
Year: 2022
Journal: Mol Cell
Title: Energy sensor AMPK gamma regulates translation via phosphatase PPP6C independent of AMPK alpha.
Volume: 82
Issue: 24
Pages: 4700-4711.e12
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Publication
33402706 | J:331776
First Author: Mossa A
Year: 2021
Journal: Mol Psychiatry
Title: Developmental impaired Akt signaling in the Shank1 and Shank3 double knock-out mice.
Volume: 26
Issue: 6
Pages: 1928-1944
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Publication
23869404 | -
First Author: Beck J
Year: 2013
Journal: Mol Microbiol
Title: Woronin bodies, their impact on stress resistance and virulence of the pathogenic mould Aspergillus fumigatus and their anchoring at the septal pore of filamentous Ascomycota.
Volume: 89
Issue: 5
Pages: 857-71
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Protein Domain
IPR001884 | IF5A-like
Type: Family
Description: Eukaryotic eIF-5A was initially thought to function as a translation initiation factor, based on its ability to stimulate methionyl-puromycin synthesis. However, subsequent work revealed a role for eIF5A in translation elongation [, ]. Depletion or inactivation of eIF-5A in the yeast Saccharomyces cerevisiae (Baker's yeast) resulted in the accumulation of polysomes and an increase in ribosomal transit times. Addition of recombinant eIF-5A from yeast, but not a derivative lacking hypusine, enhanced the rate of tripeptide synthesis in vitro. Moreover, inactivation of eIF-5A mimicked the effects of the eEF2 inhibitor sordarin, indicating that eIF-5A might function together with eEF2 to promote ribosomal translocation. Finally, it was shown that eIF5A is specifically required to promote peptide-bond formation between consecutive proline residues. It has been proposed to stimulate the peptidyl-transferase activity of the ribosome and facilitate the reactivity of poor substrates like proline [].eIF-5A is a cofactor for the Rev and Rex transactivator proteins of human immunodeficiency virus-1 and T-cell leukaemia virus I, respectively [, , ]. IF-5A is the sole protein in eukaryotes and archaea to contain the unusual amino acid hypusine (Ne-(4-amino-2-hydroxybutyl)lysine) that is an absolute functional requirement. The first step in the post-translational modification of lysine to hypusine is catalyzed by the enzyme deoxyhypusine synthase, the structure of which has been reported []. The archaeal IF-5A proteins have not been studied as comprehensively as their eukaryotic homologues, though the crystal structure of the Pyrobaculum aerophilum protein has been determined. Unmodified P. aerophilum IF-5A is found to be a beta structure with two domains and three separate hydrophobic cores. The lysine (Lys42) that is post-translationally modified by deoxyhypusine synthase is found at one end of the IF-5A molecule in a turn between beta strands beta4 and beta5; this lysine residue is freely solvent accessible.The C-terminal domain is found to be homologous to the cold-shock protein CspA of E. coli, which has a well characterised RNA-binding fold, suggesting that IF-5A is involved in RNA binding [].This family also includes the Woronin body major protein Hex1, whose sequence and structure are similar to eukaryotic initiation factor 5A (eIF5A), suggesting they share a common ancestor during evolution []. Woronin bodies are important for stress resistance and virulence [].
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Protein
Q05AH4
Organism: Mus musculus/domesticus
Length: 187  
Fragment?: false
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Publication
8347280 | -
First Author: Park MH
Year: 1993
Journal: Biofactors
Title: Hypusine: its post-translational formation in eukaryotic initiation factor 5A and its potential role in cellular regulation.
Volume: 4
Issue: 2
Pages: 95-104
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Publication
1903841 | -
First Author: Schnier J
Year: 1991
Journal: Mol Cell Biol
Title: Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae.
Volume: 11
Issue: 6
Pages: 3105-14
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Publication
23727016 | -
First Author: Gutierrez E
Year: 2013
Journal: Mol Cell
Title: eIF5A promotes translation of polyproline motifs.
Volume: 51
Issue: 1
Pages: 35-45
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Publication
28392174 | -
First Author: Schuller AP
Year: 2017
Journal: Mol Cell
Title: eIF5A Functions Globally in Translation Elongation and Termination.
Volume: 66
Issue: 2
Pages: 194-205.e5
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Publication
30876805 | -
First Author: Schopf FH
Year: 2019
Journal: Mol Cell
Title: The Co-chaperone Cns1 and the Recruiter Protein Hgh1 Link Hsp90 to Translation Elongation via Chaperoning Elongation Factor 2.
Volume: 74
Issue: 1
Pages: 73-87.e8
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Publication
11493638 | -
First Author: Crevel G
Year: 2001
Journal: J Cell Sci
Title: The Drosophila Dpit47 protein is a nuclear Hsp90 co-chaperone that interacts with DNA polymerase alpha.
Volume: 114
Issue: Pt 11
Pages: 2015-25
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Publication
18320024 | -
First Author: Crevel G
Year: 2008
Journal: PLoS One
Title: The human TPR protein TTC4 is a putative Hsp90 co-chaperone which interacts with CDC6 and shows alterations in transformed cells.
Volume: 3
Issue: 3
Pages: e0001737
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Protein Domain
IPR044059 | Csn1/TTC4_wheel
Type: Domain
Description: Co-chaperones are helper interacting proteins that modulate the chaperone cycle, being involved in substrate specificity and stimulation of chaperone activity of HSP90/70 and include other heat shock proteins, TPR containing proteins, cyclophilins and others. The TPR containing proteins possess an N-terminal TPR domain, which are more closely related to each other than to TPR domains from other proteins with different functionality [, ], which is involved in HSP90/70 direct interaction. The first N-terminal residues prior to the TRP domain and the C-terminal domain are involved and important for domain interplay and stabilisation of its interactions []. The Hsp90 chaperone machinery in eukaryotes comprises a number of distinct accessory factors, among them TTC4 from human and its homologues Cns1 from yeast and Dpit47 from Drosophila, structurally and functionally conserved from yeast to human. Cns1 is one of the few essential co-chaperones in yeast, important for maintaining translation elongation, specifically chaperoning the elongation factor eEF2. Cns1 interacts with Hgh1 and forms a quaternary complex together with eEF2 and Hsp90 mediating the proper folding and solubility of eEF2. Recently, the C-terminal structure has been solved and is called the "wheel"domain according to its 2D projection. It shows an overall fold consisting of a twisted five-stranded beta sheet surrounded by several alpha helices [].This entry represents the wheel domain found at the C terminus of yeast Cns1, human TTC4 and Drosophila Dpit47 proteins.
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Publication
37775560 | J:343230
First Author: Malik N
Year: 2023
Journal: Leukemia
Title: mTORC1-selective activation of translation elongation promotes disease progression in chronic lymphocytic leukemia.
Volume: 37
Issue: 12
Pages: 2414-2425
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Publication
33341653 | J:305533
 
First Author: Yang W
Year: 2021
Journal: Neurobiol Aging
Title: Suppression of the kinase for elongation factor 2 alleviates mGluR-LTD impairments in a mouse model of Alzheimer's disease.
Volume: 98
Pages: 225-230
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Publication
19828446 | J:158214
First Author: Ikeda Y
Year: 2009
Journal: J Biol Chem
Title: Cardiac-specific deletion of LKB1 leads to hypertrophy and dysfunction.
Volume: 284
Issue: 51
Pages: 35839-49
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Publication
25755286 | J:224411
First Author: Moore CE
Year: 2015
Journal: Mol Cell Biol
Title: Elongation Factor 2 Kinase Is Regulated by Proline Hydroxylation and Protects Cells during Hypoxia.
Volume: 35
Issue: 10
Pages: 1788-804
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Publication
29395043 | J:329167
First Author: Adaikkan C
Year: 2018
Journal: Biol Psychiatry
Title: Calcium/Calmodulin-Dependent Protein Kinase II and Eukaryotic Elongation Factor 2 Kinase Pathways Mediate the Antidepressant Action of Ketamine.
Volume: 84
Issue: 1
Pages: 65-75
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Publication
22675026 | J:198893
First Author: López-Pelaéz M
Year: 2012
Journal: Mol Biol Cell
Title: Cot/tpl2-MKK1/2-Erk1/2 controls mTORC1-mediated mRNA translation in Toll-like receptor-activated macrophages.
Volume: 23
Issue: 15
Pages: 2982-92
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Publication
22366775 | J:316669
First Author: Gildish I
Year: 2012
Journal: Learn Mem
Title: Impaired associative taste learning and abnormal brain activation in kinase-defective eEF2K mice.
Volume: 19
Issue: 3
Pages: 116-25
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Publication
29700204 | J:262780
 
First Author: Argüello RJ
Year: 2018
Journal: J Cell Sci
Title: SunRiSE - measuring translation elongation at single-cell resolution by means of flow cytometry.
Volume: 131
Issue: 10
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Publication
25623400 | J:318267
First Author: Steiner JL
Year: 2015
Journal: Alcohol Clin Exp Res
Title: Alcohol intoxication following muscle contraction in mice decreases muscle protein synthesis but not mTOR signal transduction.
Volume: 39
Issue: 1
Pages: 1-10
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Publication
12640443 | -
First Author: Yuan P
Year: 2003
Journal: Nat Struct Biol
Title: A HEX-1 crystal lattice required for Woronin body function in Neurospora crassa.
Volume: 10
Issue: 4
Pages: 264-70
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Publication
9493264 | -
First Author: Liao DI
Year: 1998
Journal: Structure
Title: Crystal structure of the NAD complex of human deoxyhypusine synthase: an enzyme with a ball-and-chain mechanism for blocking the active site.
Volume: 6
Issue: 1
Pages: 23-32
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Publication
9753699 | -
First Author: Peat TS
Year: 1998
Journal: Structure
Title: Structure of translation initiation factor 5A from Pyrobaculum aerophilum at 1.75 A resolution.
Volume: 6
Issue: 9
Pages: 1207-14
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Publication
19424157 | -
First Author: Saini P
Year: 2009
Journal: Nature
Title: Hypusine-containing protein eIF5A promotes translation elongation.
Volume: 459
Issue: 7243
Pages: 118-21
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Publication
29337352 | J:264586
First Author: Zimmermann HR
Year: 2018
Journal: J Neurochem
Title: Genetic removal of eIF2α kinase PERK in mice enables hippocampal L-LTP independent of mTORC1 activity.
Volume: 146
Issue: 2
Pages: 133-144
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Publication
24945486 | J:216832
First Author: Steiner JL
Year: 2014
Journal: PLoS One
Title: Disruption of genes encoding eIF4E binding proteins-1 and -2 does not alter basal or sepsis-induced changes in skeletal muscle protein synthesis in male or female mice.
Volume: 9
Issue: 6
Pages: e99582
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Publication
19188248 | J:176549
First Author: Rose AJ
Year: 2009
Journal: J Physiol
Title: A Ca(2+)-calmodulin-eEF2K-eEF2 signalling cascade, but not AMPK, contributes to the suppression of skeletal muscle protein synthesis during contractions.
Volume: 587
Issue: Pt 7
Pages: 1547-63
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Protein
Q66JR8
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
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Protein
Q8VHU9
Organism: Mus musculus/domesticus
Length: 61  
Fragment?: true
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Protein
Q8CH67
Organism: Mus musculus/domesticus
Length: 41  
Fragment?: true
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Protein
J3QPS8
Organism: Mus musculus/domesticus
Length: 76  
Fragment?: false
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Protein
P63242
Organism: Mus musculus/domesticus
Length: 154  
Fragment?: false
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Protein
Q8BGY2
Organism: Mus musculus/domesticus
Length: 153  
Fragment?: false
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Protein
A0A0A0MQM0
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: true
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Protein
Q8R3H9
Organism: Mus musculus/domesticus
Length: 386  
Fragment?: false
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Protein
Q8C2G3
Organism: Mus musculus/domesticus
Length: 386  
Fragment?: false
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Protein
Q3UZC4
Organism: Mus musculus/domesticus
Length: 386  
Fragment?: false
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Publication
15489334 | -
First Author: Gerhard DS
Year: 2004
Journal: Genome Res
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume: 14
Issue: 10B
Pages: 2121-7
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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Cambridge CB2 3EH, United Kingdom