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000060127 0247_ $$2DOI$$a10.1021/bi7018145
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000060127 084__ $$2WoS$$aBiochemistry & Molecular Biology
000060127 1001_ $$0P:(DE-Juel1)132012$$aMohrlüder, J.$$b0$$uFZJ
000060127 245__ $$aIdentification of clathrin heavy chain as a direct binding partner for the GABA type A receptor associated protein GABARAP
000060127 260__ $$aColumbus, Ohio$$bAmerican Chemical Society$$c2007
000060127 300__ $$a14537 - 14543
000060127 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000060127 440_0 $$0798$$aBiochemistry$$v46$$x0006-2960
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000060127 520__ $$aGamma-aminobutyric acid type A receptors (GABAA receptors) are the major sites of GABA-mediated fast synaptic inhibition in the central nervous system. Variation of the cell surface receptor count is postulated to be of importance in modulating inhibitory synaptic transmission. The GABAA receptor associated protein (GABARAP) is a ubiquitin-like modifier, implicated in GABAA receptor clustering, trafficking, and turnover. GABARAP pull-down experiments with brain lysate identified clathrin heavy chain to be GABARAP-associated. Phage display screening of a randomized peptide library for GABARAP ligands yielded a sequence motif which characterizes the peptide binding specificity of GABARAP. Sequence database searches with this motif revealed clathrin heavy chain as a protein containing the identified sequence motif within its residues 510-522, supporting the result of the pull-down experiments. Calreticulin, which was identified recently as a GABARAP ligand, contains a very similar sequence motif. We demonstrate that calreticulin indeed competes with clathrin heavy chain for GABARAP binding. Finally, employing nuclear magnetic resonance spectroscopy, we mapped the GABARAP residues responsible for binding to clathrin. The hereby mapped GABARAP regions overlap very well with the homologue residues in yeast Atg8 that were recently shown to be important for autophagy. Together with the knowledge that GABARAP and clathrin are known to be involved in GABAA receptor trafficking within the cell, this strongly suggests a clear physiological relevance of the direct interaction of GABARAP with clathrin heavy chain.
000060127 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
000060127 588__ $$aDataset connected to Web of Science, Pubmed
000060127 650_2 $$2MeSH$$aAmino Acid Sequence
000060127 650_2 $$2MeSH$$aCalreticulin: chemistry
000060127 650_2 $$2MeSH$$aCalreticulin: metabolism
000060127 650_2 $$2MeSH$$aClathrin Heavy Chains: chemistry
000060127 650_2 $$2MeSH$$aClathrin Heavy Chains: genetics
000060127 650_2 $$2MeSH$$aClathrin Heavy Chains: metabolism
000060127 650_2 $$2MeSH$$aMagnetic Resonance Spectroscopy
000060127 650_2 $$2MeSH$$aModels, Molecular
000060127 650_2 $$2MeSH$$aMolecular Sequence Data
000060127 650_2 $$2MeSH$$aProtein Binding
000060127 650_2 $$2MeSH$$aProtein Structure, Tertiary
000060127 650_2 $$2MeSH$$aReceptors, GABA-A: chemistry
000060127 650_2 $$2MeSH$$aReceptors, GABA-A: genetics
000060127 650_2 $$2MeSH$$aReceptors, GABA-A: metabolism
000060127 650_2 $$2MeSH$$aSequence Homology, Amino Acid
000060127 650_7 $$00$$2NLM Chemicals$$aCalreticulin
000060127 650_7 $$00$$2NLM Chemicals$$aReceptors, GABA-A
000060127 650_7 $$0114899-12-6$$2NLM Chemicals$$aClathrin Heavy Chains
000060127 650_7 $$2WoSType$$aJ
000060127 7001_ $$0P:(DE-Juel1)VDB65464$$aHoffmann, Y.$$b1$$uFZJ
000060127 7001_ $$0P:(DE-Juel1)VDB8627$$aStangler, T.$$b2$$uFZJ
000060127 7001_ $$0P:(DE-Juel1)VDB21605$$aHänel, K.$$b3$$uFZJ
000060127 7001_ $$0P:(DE-Juel1)132029$$aWillbold, D.$$b4$$uFZJ
000060127 773__ $$0PERI:(DE-600)1472258-6$$a10.1021/bi7018145$$gVol. 46, p. 14537 - 14543$$p14537 - 14543$$q46<14537 - 14543$$tBiochemistry$$v46$$x0006-2960$$y2007
000060127 8567_ $$uhttp://dx.doi.org/10.1021/bi7018145
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000060127 9141_ $$y2007
000060127 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000060127 9201_ $$0I:(DE-Juel1)VDB805$$d31.12.2008$$gINB$$kINB-2$$lMolekulare Biophysik$$x0
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