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- W138794641 abstract "Neuropeptides are stored in secretory granules to be released at the appropriate time in response to stimulation. Peptidylglycine á-Amidating Monooxygenase (PAM), a granule membrane protein essential for the biosynthesis of many peptides, has a cytosolic domain (PAM-CD) that controls its trafficking in both the secretory and endocytic pathways. The aim of this study was to elucidate the role of the unstructured PAM-CD in signaling via multisite phosphorylation, cleavage and nuclear translocation of a soluble fragment. The 86 amino acids long PAM-CD has 13 predicted Ser/Thr phosphorylation sites. We identified 6 of these as phosphorylation sites by mass-spectrometry and phospho-specific antibody analysis of PAM-1 in neuroendocrine AtT-20 cells. Circular dichroism showed that purified recombinant PAM-CD is unstructured. Two-dimensional gel electrophoretic analysis of AtT-20 cell extracts and primary cultures of rat anterior pituitary demonstrated that PAM-CD can be simultaneously phosphorylated at as many as 10 sites under basal conditions, generating intact protein with pI values between 4.6 and 5.2. We showed that PAM-CD was cleaved, generating a cytosolic C-terminal fragment in PAM-1 AtT-20 cells, anterior pituitary and atrium. This soluble fragment accumulated in the nucleus, possibly acting as a feedback mechanism to regulate transcription of secretory granule proteins." @default.
- W138794641 created "2016-06-24" @default.
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- W138794641 date "2009-04-01" @default.
- W138794641 modified "2023-09-26" @default.
- W138794641 title "Multisite phosphorylation, cleavage and nuclear translocation of the unstructured PAM cytosolic domain" @default.
- W138794641 doi "https://doi.org/10.1096/fasebj.23.1_supplement.706.1" @default.
- W138794641 hasPublicationYear "2009" @default.
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