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Article

Access of a membrane protein to secretory granules is facilitated by phosphorylation.

The Journal of biological chemistry - 26 Oct 2001

Steveson T C, Zhao G C, Keutmann H T, Mains R E, Eipper B A

Abstract excerpt

Peptidylglycine alpha-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 Ser(949) and Thr(946) of PAM, generating a short, cytosolic acidic cluster. P-CIP2, a protein kinase identified by its ability to interact with...

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Share to Casein Kinase II
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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 11524414
DOI: 10.1074/jbc.M011460200

Genes

PAM

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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