Structure-function relations of smooth muscle calponin. The critical role of serine 175

Calponin has been implicated in the regulation of smooth muscle contraction through its interaction with F-actin and inhibition of the actin-activated MgATPase activity of phosphorylated myosin. Both properties are lost following phosphorylation (primarily at serine 175) by protein kinase C or calmo...

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Veröffentlicht in:	The Journal of biological chemistry 1996-04, Vol.271 (15), p.8605
Hauptverfasser:	Tang, D C, Kang, H M, Jin, J P, Fraser, E D, Walsh, M P
Format:	Artikel
Sprache:	eng
Schlagworte:	Actins - metabolism Animals Base Sequence Calcium-Binding Proteins - chemistry Calcium-Binding Proteins - metabolism Calcium-Calmodulin-Dependent Protein Kinase Type 2 Calcium-Calmodulin-Dependent Protein Kinases - metabolism Calponins Chickens DNA Primers - chemistry Enzyme Activation Epitope Mapping Microfilament Proteins - chemistry Molecular Sequence Data Muscle Proteins - chemistry Muscle Proteins - metabolism Muscle, Smooth - chemistry Mutagenesis, Site-Directed Myosins - metabolism Peptide Mapping Phosphorylation Protein Kinase C - metabolism Rats Recombinant Proteins Serine - chemistry Structure-Activity Relationship
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