Identification of chromaffin granule-binding proteins. Relationship of the chromobindins to calelectrin, synhibin, and the tyrosine kinase substrates p35 and p36.

Creutz, Carl E.; Zaks, William J.; Hamman, Helen C.; Crane, Sharon; Martin, William H.; Gould, Kathleen L.; Oddie, K M; Parsons, Sarah J.

doi:10.1016/s0021-9258(19)75719-6

Cited by 170 publications

(17 citation statements)

References 54 publications

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“…Thiophosphorylated proteins are known to be relatively resistant to cellular phosphatases (Eckstein, 1985) . Our interpretation of these results is that the involvement of calpactin in the exocytotic machinery requires phosphorylation by protein kinase C. Calpactin I was previously identified by Creutz et al (1987) among the chromobindins, a group of soluble proteins ofthe adrenal medulla that bind to the chromaffin granule membrane in a calcium-dependent way (Creutz et al ., 1983). Calpactin was found to undergo phosphorylation predominantly on serine residues during stimulation of chromaffin cells with nicotine (Creutz et al, 1987) .…”

Section: Discussionmentioning

confidence: 75%

“…Our interpretation of these results is that the involvement of calpactin in the exocytotic machinery requires phosphorylation by protein kinase C. Calpactin I was previously identified by Creutz et al (1987) among the chromobindins, a group of soluble proteins ofthe adrenal medulla that bind to the chromaffin granule membrane in a calcium-dependent way (Creutz et al ., 1983). Calpactin was found to undergo phosphorylation predominantly on serine residues during stimulation of chromaffin cells with nicotine (Creutz et al, 1987) . Since protein kinase C is activated during nicotinic stimulation (Terbush and Holz, 1986), it becomes a good candidate for mediating the phosphorylation of calpactin during exocytosis.…”

Section: Discussionmentioning

confidence: 75%

“…Since protein kinase C is activated during nicotinic stimulation (Terbush and Holz, 1986), it becomes a good candidate for mediating the phosphorylation of calpactin during exocytosis. In addition Creutz et al . (1987) observed in several experiments traces of alkali-resistant phosphorylation of calpactin after nicotinic stimulation, suggesting that some phosphorylation on tyrosine residues may also occur.…”

Section: Discussionmentioning

confidence: 99%

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The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C.

Sarafian

Pradel

Henry

et al. 1991

The Journal of Cell Biology

185

118

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Section: Discussionmentioning

confidence: 75%

Section: Discussionmentioning

confidence: 75%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C.

Sarafian

Pradel

Henry

et al. 1991

The Journal of Cell Biology

185

118

View full text Add to dashboard Cite

show abstract

“…One-dimensional isoelectric focusing was performed using a discontinuous buffer method in an SE 600 vertical slab gel unit (Hoefer Scientific Instruments) and pH 4-6 ampholytes (protocol of Gary Giulian, University of Wisconsin, described in the Hoeffer 1992-1993 catalog). Western blots were performed as previously described using a horseradish peroxidase colordeveloping system (Creutz et al, 1987). Minilysate plasmid preparations and major plasmid preparations utilizing polyethylene glycol) precipitations were conducted according to standard molecular biology techniques (Ausubel et al, 1989).…”

Section: Methodsmentioning

confidence: 99%

Combinatorial Mutagenesis of the Four Domains of Annexin IV: Effects on Chromaffin Granule Binding and Aggregating Activities

Nelson

Creutz²

1995

Biochemistry

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This study addresses the roles of individual annexin IV domains in calcium-dependent membrane binding and aggregation through an analysis of the activities of mutant annexin IV proteins in which critical residues in one or more domains have been altered. The consensus sequence for high-affinity Ca(2+)-binding pockets obtained from the annexin V crystal structure is GXGT-38 residues-D/E [Huber, R., et al. (1992) J. Mol. Biol. 223, 683-704]. Site-directed mutagenesis was used to change the conserved acidic residues (D/E) in these sequences to alanine residues in each of the four domains of bovine annexin IV, singly or in combinations. Fourteen mutants with one, two, three, or four mutated domains were constructed and expressed in Escherichia coli. Purified recombinant product was evaluated for Ca(2+)-dependent binding to and aggregation of bovine chromaffin granules. Increases in the number of mutated domains resulted in increased Ca2+ requirements for both granule binding and aggregation. Further analysis revealed that mutations in individual domains had preferential effects on the binding or aggregating activities of the protein. For example, mutation of the first or fourth domains had a greater effect on membrane binding than aggregation, while conversely, mutation of the second domain had a more dramatic effect on membrane aggregation. Mutation of the third domain was largely silent in these assays. An additional mutation was made in the fourth domain to substitute a serine for a highly conserved arginine residue (Arg274) present at the C-terminus of the fourth endonexin fold. This mutation increased the calcium requirement for membrane binding 2-fold and for membrane aggregation 3-fold. This mutant protein was found to be an effective inhibitor of membrane aggregation by native annexin IV at intermediate levels of calcium.

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“…Essa família de proteínas possui diversos membros, cuja identificação ocorreu principalmente nas décadas de 1970 e 1980, como resultado de uma intensa busca por proteínas que pudessem atuar como "pontes" (GERKE; MOSS, 2002). As anexinas receberam diversos nomes não-relacionados durante esse período de descobrimento, já que não havia uma relação direta traçada entre os diferentes componentes dessa família, e a maioria desses nomes fazia referência às propriedades bioquímicas dessas proteínas, como synexin (agregação de grânulos (CREUTZ; PAZOLES; POLLARD, 1978), chromobindins (proteínas que se ligam a grânulos cromafins (CREUTZ et al, 1987), calcimedins (proteínas mediadoras de sinais de cálcio (MOORE; KRAUS-FRIEDMANN; DEDMAN, 1984), lipocortins (inibidores de lipase induzidos por esteroide (FLOWER, 1986) e calpactins (proteínas que se ligam a íons Ca 2+ , fosfolipídeos e actina (GLENNEY; TACK; POWELL, 1987).…”

Section: Anexina A5 E Seu Papel Na Mineralizaçãounclassified

Efeito da Anexina A5 na interação entre íons Ca>sup<2+>/sup< e membranas contendo DPPS

Ferreira¹

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A Deus pela vida, e sobretudo pelo amparo nos momentos em que se falta algo no qual se possa agarrar.Às mulheres da minha vida, minha mãe Solange e minhas irmãs, Letícia e Vitória, por serem tão fundamentais na minha vida, e por me ensinarem sobre as coisas que importam. Todo o amor no mundo é meu, pra vocês.À minha tia Roseli, que me acolheu em sua casa desde a graduação até boa parte do mestrado, sempre muito bondosa e prestativa. Às minhas queridas primas, Rafaela e Graziela, por todos os momentos que tivemos, e ao meu tio Cleiton, pelas valiosas lições de vida que me passou. A todos vocês, minha eterna gratidão! À Dona Maria e Sérgio, por me aceitarem em sua casa durante a graduação, e por terem me incluído na família de vocês. À Maria, obrigado por todas as longas conversas e por ser sempre solícita.Ao meu orientador, Prof. Pietro, pela confiança e ótima convivência no dia-a-dia, isso fez e faz toda a diferença. Agradeço também por ser um exemplo de pessoa e de profissional, e por me mostrar as coisas que realmente importam e que valem a pena. À Maytê, pela co-orientação e aprendizado.Aos meus colegas de laboratório, Luiz, Kel, Heitor, Bruno Favarin, Bruno Molero, Fábio e Jesaías, pela convivência e pelos momentos de descontração. Obrigado por serem tão prestativos e dispostos a ajudar. Luiz, muito obrigado por ser um amigo tão presente e acolhedor. Sua alegria constante é (quase) sempre bem-vinda! Obrigado por sempre me acompanhar em tudo, você é luz! Kel, muito obrigado por todos os nossos passeios, cookies e por ser essa pessoa amável e solícita. Sou muito grato pela sua amizade! Aos meus queridos amigos do

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Identification of chromaffin granule-binding proteins. Relationship of the chromobindins to calelectrin, synhibin, and the tyrosine kinase substrates p35 and p36.

Cited by 170 publications

References 54 publications

The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C.

The participation of annexin II (calpactin I) in calcium-evoked exocytosis requires protein kinase C.

Combinatorial Mutagenesis of the Four Domains of Annexin IV: Effects on Chromaffin Granule Binding and Aggregating Activities

Efeito da Anexina A5 na interação entre íons Ca>sup<2+>/sup< e membranas contendo DPPS

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