A Factor with a Zinc- and Phorbol Ester-Binding Domain Is Necessary for Endosome Fusion

An inhibitory effect of several zinc chelators on endosome fusion reconstituted in anin vitrosystem has been recently reported (A. Aballayet al.,1995,Biochem. J.312, 919–923). The factor that requires zinc for its activity is still unknown. Since the regulatory domain of protein kinase C (PKC) conta...

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Veröffentlicht in:	Experimental cell research 1997-08, Vol.235 (1), p.28-34
Hauptverfasser:	Aballay, Alejandro, Arenas, Nora G., Quest, Andrew F.G., Mayorga, Luis S.
Format:	Artikel
Sprache:	eng
Schlagworte:	Alkaloids Animals Benzophenanthridines Binding Sites Cell Line Cysteine Endosomes - drug effects Endosomes - physiology Enzyme Inhibitors - pharmacology Isoenzymes - antagonists & inhibitors Isoenzymes - biosynthesis Isoenzymes - metabolism Kinetics Macrophages Membrane Fusion - drug effects Membrane Fusion - physiology Naphthalenes - pharmacology Peptide Fragments - biosynthesis Peptide Fragments - metabolism Phenanthridines - pharmacology Protein Kinase C - antagonists & inhibitors Protein Kinase C - biosynthesis Protein Kinase C - metabolism Recombinant Fusion Proteins - biosynthesis Recombinant Fusion Proteins - metabolism Staurosporine - pharmacology Tetradecanoylphorbol Acetate - metabolism Tetradecanoylphorbol Acetate - pharmacology Zinc - metabolism Zinc - pharmacology
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