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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},
}