001     60127
005     20200402210440.0
024 7 _ |2 pmid
|a pmid:18027972
024 7 _ |2 DOI
|a 10.1021/bi7018145
024 7 _ |2 WOS
|a WOS:000251547700020
037 _ _ |a PreJuSER-60127
041 _ _ |a eng
082 _ _ |a 570
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Mohrlüder, J.
|b 0
|u FZJ
|0 P:(DE-Juel1)132012
245 _ _ |a Identification of clathrin heavy chain as a direct binding partner for the GABA type A receptor associated protein GABARAP
260 _ _ |a Columbus, Ohio
|b American Chemical Society
|c 2007
300 _ _ |a 14537 - 14543
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Biochemistry
|x 0006-2960
|0 798
|v 46
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Gamma-aminobutyric acid type A receptors (GABAA receptors) are the major sites of GABA-mediated fast synaptic inhibition in the central nervous system. Variation of the cell surface receptor count is postulated to be of importance in modulating inhibitory synaptic transmission. The GABAA receptor associated protein (GABARAP) is a ubiquitin-like modifier, implicated in GABAA receptor clustering, trafficking, and turnover. GABARAP pull-down experiments with brain lysate identified clathrin heavy chain to be GABARAP-associated. Phage display screening of a randomized peptide library for GABARAP ligands yielded a sequence motif which characterizes the peptide binding specificity of GABARAP. Sequence database searches with this motif revealed clathrin heavy chain as a protein containing the identified sequence motif within its residues 510-522, supporting the result of the pull-down experiments. Calreticulin, which was identified recently as a GABARAP ligand, contains a very similar sequence motif. We demonstrate that calreticulin indeed competes with clathrin heavy chain for GABARAP binding. Finally, employing nuclear magnetic resonance spectroscopy, we mapped the GABARAP residues responsible for binding to clathrin. The hereby mapped GABARAP regions overlap very well with the homologue residues in yeast Atg8 that were recently shown to be important for autophagy. Together with the knowledge that GABARAP and clathrin are known to be involved in GABAA receptor trafficking within the cell, this strongly suggests a clear physiological relevance of the direct interaction of GABARAP with clathrin heavy chain.
536 _ _ |a Funktion und Dysfunktion des Nervensystems
|c P33
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK409
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Amino Acid Sequence
650 _ 2 |2 MeSH
|a Calreticulin: chemistry
650 _ 2 |2 MeSH
|a Calreticulin: metabolism
650 _ 2 |2 MeSH
|a Clathrin Heavy Chains: chemistry
650 _ 2 |2 MeSH
|a Clathrin Heavy Chains: genetics
650 _ 2 |2 MeSH
|a Clathrin Heavy Chains: metabolism
650 _ 2 |2 MeSH
|a Magnetic Resonance Spectroscopy
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Molecular Sequence Data
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary
650 _ 2 |2 MeSH
|a Receptors, GABA-A: chemistry
650 _ 2 |2 MeSH
|a Receptors, GABA-A: genetics
650 _ 2 |2 MeSH
|a Receptors, GABA-A: metabolism
650 _ 2 |2 MeSH
|a Sequence Homology, Amino Acid
650 _ 7 |0 0
|2 NLM Chemicals
|a Calreticulin
650 _ 7 |0 0
|2 NLM Chemicals
|a Receptors, GABA-A
650 _ 7 |0 114899-12-6
|2 NLM Chemicals
|a Clathrin Heavy Chains
650 _ 7 |a J
|2 WoSType
700 1 _ |a Hoffmann, Y.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB65464
700 1 _ |a Stangler, T.
|b 2
|u FZJ
|0 P:(DE-Juel1)VDB8627
700 1 _ |a Hänel, K.
|b 3
|u FZJ
|0 P:(DE-Juel1)VDB21605
700 1 _ |a Willbold, D.
|b 4
|u FZJ
|0 P:(DE-Juel1)132029
773 _ _ |a 10.1021/bi7018145
|g Vol. 46, p. 14537 - 14543
|p 14537 - 14543
|q 46<14537 - 14543
|0 PERI:(DE-600)1472258-6
|t Biochemistry
|v 46
|y 2007
|x 0006-2960
856 7 _ |u http://dx.doi.org/10.1021/bi7018145
909 C O |o oai:juser.fz-juelich.de:60127
|p VDB
913 1 _ |k P33
|v Funktion und Dysfunktion des Nervensystems
|l Funktion und Dysfunktion des Nervensystems
|b Gesundheit
|0 G:(DE-Juel1)FUEK409
|x 0
914 1 _ |y 2007
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k INB-2
|l Molekulare Biophysik
|d 31.12.2008
|g INB
|0 I:(DE-Juel1)VDB805
|x 0
920 1 _ |k JARA-SIM
|l Jülich-Aachen Research Alliance - Simulation Sciences
|g JARA
|0 I:(DE-Juel1)VDB1045
|x 1
970 _ _ |a VDB:(DE-Juel1)94327
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ISB-2-20090406
980 _ _ |a I:(DE-Juel1)VDB1045
980 _ _ |a UNRESTRICTED
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ISB-2-20090406
981 _ _ |a I:(DE-Juel1)VDB1045
981 _ _ |a I:(DE-Juel1)ICS-6-20110106


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