Access of a Membrane Protein to Secretory Granules Is Facilitated by Phosphorylation

Peptidylglycine α-amidating monooxygenase (PAM), an integral membrane protein essential for the biosynthesis of amidated peptides, was used to assess the role of cytosolic acidic clusters in trafficking to regulated secretory granules. Casein kinase II phosphorylates Ser949 and Thr946 of PAM, genera...

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Veröffentlicht in:	The Journal of biological chemistry 2001-10, Vol.276 (43), p.40326-40337
Hauptverfasser:	Steveson, Tami C., Zhao, George C., Keutmann, Henry T., Mains, Richard E., Eipper, Betty A.
Format:	Artikel
Sprache:	eng
Schlagworte:	Casein Kinase II Dichlororibofuranosylbenzimidazole - pharmacology Endocytosis Endosomes - metabolism Membrane Proteins - genetics Membrane Proteins - metabolism Mixed Function Oxygenases - genetics Mixed Function Oxygenases - metabolism Models, Biological monooxygenase Multienzyme Complexes - genetics Multienzyme Complexes - metabolism Mutation P-CIP2 protein PAM-1 protein Peptide Fragments - genetics Peptide Fragments - metabolism Peptidylglycine ^a-amidating monooxygenase Phosphorylation Protein Sorting Signals Protein Transport Protein-Serine-Threonine Kinases - metabolism Recombinant Proteins - metabolism secretory granules Secretory Vesicles - metabolism Serine - metabolism Threonine - metabolism trans-Golgi Network - metabolism
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