Protein kinase C is regulated in vivo by three functionally distinct phosphorylations

Background: Protein kinase Cs are a family of enzymes that transduce the plethora of signals promoting lipid hydrolysis. Here, we show that protein kinase C must first be processed by three distinct phosphorylations before it is competent to respond to second messengers. Results We have identified t...

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Veröffentlicht in:	Current biology 1995-12, Vol.5 (12), p.1394-1403
Hauptverfasser:	Keranen, Lisa M., Dutil, Erica M., Newton, Alexandra C.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Animals Binding Sites Cell Line Models, Molecular Molecular Sequence Data Phosphoric Monoester Hydrolases - metabolism Phosphorylation Phosphotransferases - chemistry Phosphotransferases - metabolism Protein Kinase C - metabolism Protein Kinase C beta Spodoptera - cytology Structure-Activity Relationship
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