Hauptseite > Publikationsdatenbank > Irregular dimerization of guanylate cyclase-activating protein 1 mutants causes loss of target activation > print

001     41869
005     20200402205821.0
024 7 _ |2 pmid
|a pmid:15355355
024 7 _ |2 DOI
|a 10.1111/j.1432-1033.2004.04320.x
024 7 _ |2 WOS
|a WOS:000223711400017
024 7 _ |a 0014-2956
|2 ISSN
037 _ _ |a PreJuSER-41869
041 _ _ |a eng
082 _ _ |a 540
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
100 1 _ |a Hwang, J.-Y.
|b 0
|u FZJ
|0 P:(DE-Juel1)VDB2543
245 _ _ |a Irregular dimerization of guanylate cyclase-activating protein 1 mutants causes loss of target activation
260 _ _ |c 2004
|a Oxford [u.a.]
|b Wiley-Blackwell
300 _ _ |a 3785 - 3793
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 European Journal of Biochemistry
|x 0014-2956
|0 1916
|y 18
|v 271
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Guanylate cyclase-activating proteins (GCAPs) are neuronal calcium sensors that activate membrane bound guanylate cyclases (EC 4.6.1.2.) of vertebrate photoreceptor cells when cytoplasmic Ca2+ decreases during illumination. GCAPs contain four EF-hand Ca2+-binding motifs, but the first EF-hand is nonfunctional. It was concluded that for GCAP-2, the loss of Ca2+-binding ability of EF-hand 1 resulted in a region that is crucial for targeting guanylate cyclase [Ermilov, A.N., Olshevskaya, E.V. & Dizhoor, A.M. (2001) J. Biol. Chem.276, 48143-48148]. In this study we tested the consequences of mutations in EF-hand 1 of GCAP-1 with respect to Ca2+ binding, Ca2+-induced conformational changes and target activation. When the nonfunctional first EF-hand in GCAP-1 is replaced by a functional EF-hand the chimeric mutant CaM-GCAP-1 bound four Ca2+ and showed similar Ca2+-dependent changes in tryptophan fluorescence as the wild-type. CaM-GCAP-1 neither activated nor interacted with guanylate cyclase. Size exclusion chromatography revealed that the mutant tended to form inactive dimers instead of active monomers like the wild-type. Critical amino acids in EF-hand 1 of GCAP-1 are cysteine at position 29 and proline at position 30, as changing these to glycine was sufficient to cause loss of target activation without a loss of Ca2+-induced conformational changes. The latter mutation also promoted dimerization of the protein. Our results show that EF-hand 1 in wild-type GCAP-1 is critical for providing the correct conformation for target activation.
536 _ _ |a Neurowissenschaften
|c L01
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK255
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Amino Acid Sequence
650 _ 2 |2 MeSH
|a Animals
650 _ 2 |2 MeSH
|a Calcium: metabolism
650 _ 2 |2 MeSH
|a Calcium-Binding Proteins: chemistry
650 _ 2 |2 MeSH
|a Calcium-Binding Proteins: genetics
650 _ 2 |2 MeSH
|a Calcium-Binding Proteins: isolation & purification
650 _ 2 |2 MeSH
|a Calcium-Binding Proteins: metabolism
650 _ 2 |2 MeSH
|a Chromatography, Gel
650 _ 2 |2 MeSH
|a Cysteine: metabolism
650 _ 2 |2 MeSH
|a Dimerization
650 _ 2 |2 MeSH
|a EF Hand Motifs: genetics
650 _ 2 |2 MeSH
|a Escherichia coli: genetics
650 _ 2 |2 MeSH
|a Guanylate Cyclase-Activating Proteins
650 _ 2 |2 MeSH
|a Light Signal Transduction
650 _ 2 |2 MeSH
|a Molecular Sequence Data
650 _ 2 |2 MeSH
|a Mutation
650 _ 2 |2 MeSH
|a Proline: metabolism
650 _ 2 |2 MeSH
|a Protein Conformation
650 _ 2 |2 MeSH
|a Reactive Oxygen Species: metabolism
650 _ 2 |2 MeSH
|a Recombinant Proteins: chemistry
650 _ 2 |2 MeSH
|a Recombinant Proteins: metabolism
650 _ 2 |2 MeSH
|a Sequence Homology, Amino Acid
650 _ 2 |2 MeSH
|a Spectrometry, Fluorescence
650 _ 7 |0 0
|2 NLM Chemicals
|a Calcium-Binding Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Guanylate Cyclase-Activating Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Reactive Oxygen Species
650 _ 7 |0 0
|2 NLM Chemicals
|a Recombinant Proteins
650 _ 7 |0 147-85-3
|2 NLM Chemicals
|a Proline
650 _ 7 |0 52-90-4
|2 NLM Chemicals
|a Cysteine
650 _ 7 |0 7440-70-2
|2 NLM Chemicals
|a Calcium
650 _ 7 |a J
|2 WoSType
653 2 0 |2 Author
|a GCAP
653 2 0 |2 Author
|a guanylate cyclase
653 2 0 |2 Author
|a neuronal Ca2+ sensor
653 2 0 |2 Author
|a phototransduction
700 1 _ |a Schlesinger, R.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB1421
700 1 _ |a Koch, K.-W.
|b 2
|u FZJ
|0 P:(DE-Juel1)VDB789
773 _ _ |0 PERI:(DE-600)2172518-4
|a 10.1111/j.1432-1033.2004.04320.x
|g Vol. 271, p. 3785 - 3793
|p 3785 - 3793
|q 271<3785 - 3793
|t The @FEBS journal
|v 271
|x 0014-2956
|y 2004
856 7 _ |u http://dx.doi.org/10.1111/j.1432-1033.2004.04320.x
909 C O |o oai:juser.fz-juelich.de:41869
|p VDB
913 1 _ |k L01
|v Neurowissenschaften
|l Funktion und Dysfunktion des Nervensystems
|b Leben
|0 G:(DE-Juel1)FUEK255
|x 0
914 1 _ |y 2004
915 _ _ |a JCR/ISI refereed
|0 StatID:(DE-HGF)0010
|2 StatID
915 _ _ |a JCR
|0 StatID:(DE-HGF)0100
|2 StatID
915 _ _ |a WoS
|0 StatID:(DE-HGF)0111
|2 StatID
|b Science Citation Index Expanded
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0150
|2 StatID
|b Web of Science Core Collection
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0199
|2 StatID
|b Thomson Reuters Master Journal List
915 _ _ |a DBCoverage
|0 StatID:(DE-HGF)0300
|2 StatID
|b Medline
920 1 _ |k IBI-1
|l Zelluläre Signalverarbeitung
|d 31.12.2006
|g IBI
|0 I:(DE-Juel1)VDB57
|x 0
920 1 _ |k IBI-2
|l Biologische Strukturforschung
|d 31.12.2006
|g IBI
|0 I:(DE-Juel1)VDB58
|x 1
970 _ _ |a VDB:(DE-Juel1)58127
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ICS-4-20110106
980 _ _ |a I:(DE-Juel1)ISB-2-20090406
980 _ _ |a UNRESTRICTED
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
981 _ _ |a I:(DE-Juel1)IBI-1-20200312
981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ICS-4-20110106
981 _ _ |a I:(DE-Juel1)ISB-2-20090406
981 _ _ |a I:(DE-Juel1)ICS-6-20110106

LibraryCollectionCLSMajorCLSMinorLanguageAuthor
Marc 21