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Phosphorylation of calmodulin on Tyr99 selectively attenuates the action of calmodulin antagonists on type-I cyclic nucleotide phosphodiesterase activity.

Tyr99 phosphorylation of calmodulin appears to induce a distinct conformational change as is evident from the profound attenuation of the Ca(2+)-induced enhancement of calmodulin's mobility seen during SDS/PAGE. The effect of this conformational change appears to be localized, in that both calm...

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Detalhes bibliográficos
Main Authors: Saville, M K, Houslay, M D
Formato: Artigo
Idioma:Inglês
Publicado em: 1994
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC1138100/
https://ncbi.nlm.nih.gov/pubmed/8192677
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