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@ARTICLE{Mohrlder:60127,
author = {Mohrlüder, J. and Hoffmann, Y. and Stangler, T. and
Hänel, K. and Willbold, D.},
title = {{I}dentification of clathrin heavy chain as a direct
binding partner for the {GABA} type {A} receptor associated
protein {GABARAP}},
journal = {Biochemistry},
volume = {46},
issn = {0006-2960},
address = {Columbus, Ohio},
publisher = {American Chemical Society},
reportid = {PreJuSER-60127},
pages = {14537 - 14543},
year = {2007},
note = {Record converted from VDB: 12.11.2012},
abstract = {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.},
keywords = {Amino Acid Sequence / Calreticulin: chemistry /
Calreticulin: metabolism / Clathrin Heavy Chains: chemistry
/ Clathrin Heavy Chains: genetics / Clathrin Heavy Chains:
metabolism / Magnetic Resonance Spectroscopy / Models,
Molecular / Molecular Sequence Data / Protein Binding /
Protein Structure, Tertiary / Receptors, GABA-A: chemistry /
Receptors, GABA-A: genetics / Receptors, GABA-A: metabolism
/ Sequence Homology, Amino Acid / Calreticulin (NLM
Chemicals) / Receptors, GABA-A (NLM Chemicals) / Clathrin
Heavy Chains (NLM Chemicals) / J (WoSType)},
cin = {INB-2 / JARA-SIM},
ddc = {570},
cid = {I:(DE-Juel1)VDB805 / I:(DE-Juel1)VDB1045},
pnm = {Funktion und Dysfunktion des Nervensystems},
pid = {G:(DE-Juel1)FUEK409},
shelfmark = {Biochemistry $\&$ Molecular Biology},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:18027972},
UT = {WOS:000251547700020},
doi = {10.1021/bi7018145},
url = {https://juser.fz-juelich.de/record/60127},
}