Hauptseite > Publikationsdatenbank > Identification of calreticulin as ligand of GABARAP by phage display screening of a peptide library > print

001     60125
005     20200423204551.0
024 7 _ |2 pmid
|a pmid:17916189
024 7 _ |2 DOI
|a 10.1111/j.1742-4658.2007.06073.x
024 7 _ |2 WOS
|a WOS:000250297600009
024 7 _ |a 2128/4688
|2 Handle
024 7 _ |2 Handle
|a 2128/4687
037 _ _ |a PreJuSER-60125
041 _ _ |a eng
082 _ _ |a 540
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 calreticulin as ligand of GABARAP by phage display screening of a peptide library
260 _ _ |a Oxford [u.a.]
|b Wiley-Blackwell
|c 2007
300 _ _ |a 5543 - 5555
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 FEBS Journal
|x 1742-464X
|0 17341
|v 274
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a 4-Aminobutyrate type A (GABA(A)) receptor-associated protein (GABARAP) is a ubiquitin-like modifier implicated in the intracellular trafficking of GABA(A) receptors, and belongs to a family of proteins involved in intracellular vesicular transport processes, such as autophagy and intra-Golgi transport. In this article, it is demonstrated that calreticulin is a high affinity ligand of GABARAP. Calreticulin, although best known for its functions as a Ca(2+) -dependent chaperone and a Ca(2+) -buffering protein in the endoplasmic reticulum, is also localized to the cytosol and exerts a variety of extra-endoplasmic reticulum functions. By phage display screening of a randomized peptide library, peptides that specifically bind GABARAP were identified. Their amino acid sequences allowed us to identify calreticulin as a potential GABARAP binding protein. GABARAP binding to calreticulin was confirmed by pull-down experiments with brain lysate and colocalization studies in N2a cells. Calreticulin and GABARAP interact with a dissociation constant K(d) = 64 nm and a mean lifetime of the complex of 20 min. Thus, the interaction between GABARAP and calreticulin is the strongest so far reported for each protein.
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 Motifs
650 _ 2 |2 MeSH
|a Amino Acid Sequence
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Binding Sites
650 _ 2 |2 MeSH
|a Calreticulin: chemistry
650 _ 2 |2 MeSH
|a Calreticulin: metabolism
650 _ 2 |2 MeSH
|a Cells, Cultured
650 _ 2 |2 MeSH
|a Immunohistochemistry
650 _ 2 |2 MeSH
|a Ligands
650 _ 2 |2 MeSH
|a Microtubule-Associated Proteins: chemistry
650 _ 2 |2 MeSH
|a Microtubule-Associated Proteins: metabolism
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Molecular Sequence Data
650 _ 2 |2 MeSH
|a Peptide Fragments: chemistry
650 _ 2 |2 MeSH
|a Peptide Fragments: metabolism
650 _ 2 |2 MeSH
|a Peptide Library
650 _ 2 |2 MeSH
|a Rats
650 _ 2 |2 MeSH
|a Surface Plasmon Resonance
650 _ 7 |0 0
|2 NLM Chemicals
|a Calreticulin
650 _ 7 |0 0
|2 NLM Chemicals
|a GABARAP protein, rat
650 _ 7 |0 0
|2 NLM Chemicals
|a Ligands
650 _ 7 |0 0
|2 NLM Chemicals
|a Microtubule-Associated Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Peptide Fragments
650 _ 7 |0 0
|2 NLM Chemicals
|a Peptide Library
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a calreticulin
653 2 0 |2 Author
|a GABA(A) receptor
653 2 0 |2 Author
|a GABARAP
653 2 0 |2 Author
|a phage display screening
653 2 0 |2 Author
|a protein-protein interaction
700 1 _ |a Stangler, T.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB8627
700 1 _ |a Wiesehan, K.
|b 2
|u FZJ
|0 P:(DE-Juel1)VDB15437
700 1 _ |a Hoffmann, Y.
|b 3
|u FZJ
|0 P:(DE-Juel1)VDB65464
700 1 _ |a Mataruga, A.
|b 4
|u FZJ
|0 P:(DE-Juel1)VDB64411
700 1 _ |a Willbold, D.
|b 5
|u FZJ
|0 P:(DE-Juel1)132029
773 _ _ |a 10.1111/j.1742-4658.2007.06073.x
|g Vol. 274, p. 5543 - 5555
|p 5543 - 5555
|q 274<5543 - 5555
|0 PERI:(DE-600)2172518-4
|t The @FEBS journal
|v 274
|y 2007
|x 1742-464X
|n 21
856 7 _ |u http://dx.doi.org/10.1111/j.1742-4658.2007.06073.x
856 4 _ |u https://juser.fz-juelich.de/record/60125/files/4688.pdf
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