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000041869 0247_ $$2DOI$$a10.1111/j.1432-1033.2004.04320.x
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000041869 084__ $$2WoS$$aBiochemistry & Molecular Biology
000041869 1001_ $$0P:(DE-Juel1)VDB2543$$aHwang, J.-Y.$$b0$$uFZJ
000041869 245__ $$aIrregular dimerization of guanylate cyclase-activating protein 1 mutants causes loss of target activation
000041869 260__ $$aOxford [u.a.]$$bWiley-Blackwell$$c2004
000041869 300__ $$a3785 - 3793
000041869 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000041869 440_0 $$01916$$aEuropean Journal of Biochemistry$$v271$$x0014-2956$$y18
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000041869 520__ $$aGuanylate 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.
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000041869 650_2 $$2MeSH$$aAmino Acid Sequence
000041869 650_2 $$2MeSH$$aAnimals
000041869 650_2 $$2MeSH$$aCalcium: metabolism
000041869 650_2 $$2MeSH$$aCalcium-Binding Proteins: chemistry
000041869 650_2 $$2MeSH$$aCalcium-Binding Proteins: genetics
000041869 650_2 $$2MeSH$$aCalcium-Binding Proteins: isolation & purification
000041869 650_2 $$2MeSH$$aCalcium-Binding Proteins: metabolism
000041869 650_2 $$2MeSH$$aChromatography, Gel
000041869 650_2 $$2MeSH$$aCysteine: metabolism
000041869 650_2 $$2MeSH$$aDimerization
000041869 650_2 $$2MeSH$$aEF Hand Motifs: genetics
000041869 650_2 $$2MeSH$$aEscherichia coli: genetics
000041869 650_2 $$2MeSH$$aGuanylate Cyclase-Activating Proteins
000041869 650_2 $$2MeSH$$aLight Signal Transduction
000041869 650_2 $$2MeSH$$aMolecular Sequence Data
000041869 650_2 $$2MeSH$$aMutation
000041869 650_2 $$2MeSH$$aProline: metabolism
000041869 650_2 $$2MeSH$$aProtein Conformation
000041869 650_2 $$2MeSH$$aReactive Oxygen Species: metabolism
000041869 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000041869 650_2 $$2MeSH$$aRecombinant Proteins: metabolism
000041869 650_2 $$2MeSH$$aSequence Homology, Amino Acid
000041869 650_2 $$2MeSH$$aSpectrometry, Fluorescence
000041869 650_7 $$00$$2NLM Chemicals$$aCalcium-Binding Proteins
000041869 650_7 $$00$$2NLM Chemicals$$aGuanylate Cyclase-Activating Proteins
000041869 650_7 $$00$$2NLM Chemicals$$aReactive Oxygen Species
000041869 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000041869 650_7 $$0147-85-3$$2NLM Chemicals$$aProline
000041869 650_7 $$052-90-4$$2NLM Chemicals$$aCysteine
000041869 650_7 $$07440-70-2$$2NLM Chemicals$$aCalcium
000041869 650_7 $$2WoSType$$aJ
000041869 65320 $$2Author$$aGCAP
000041869 65320 $$2Author$$aguanylate cyclase
000041869 65320 $$2Author$$aneuronal Ca2+ sensor
000041869 65320 $$2Author$$aphototransduction
000041869 7001_ $$0P:(DE-Juel1)VDB1421$$aSchlesinger, R.$$b1$$uFZJ
000041869 7001_ $$0P:(DE-Juel1)VDB789$$aKoch, K.-W.$$b2$$uFZJ
000041869 773__ $$0PERI:(DE-600)2172518-4$$a10.1111/j.1432-1033.2004.04320.x$$gVol. 271, p. 3785 - 3793$$p3785 - 3793$$q271<3785 - 3793$$tThe @FEBS journal$$v271$$x0014-2956$$y2004
000041869 8567_ $$uhttp://dx.doi.org/10.1111/j.1432-1033.2004.04320.x
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