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Article

Luminal interaction of phogrin with carboxypeptidase E for effective targeting to secretory granules.

Traffic (Copenhagen, Denmark) - 1 Apr 2011

Saito Naoya, Takeuchi Toshiyuki, Kawano Ayumi, Hosaka Masahiro, Hou Ni, Torii Seiji

Abstract excerpt

Phogrin, a receptor tyrosine phosphatase-like protein, is localized to dense-core secretory granules (SGs) in various neuroendocrine cells. A previous report showed that the N-terminal luminal domain mediates targeting of this protein to SGs in AtT-20 cells. Here, we show that the luminal domain specifically interacts with carboxypeptidase E (CPE), one of the key proteins involved in peptide hormone sorting, in a...

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Share to Adaptor Proteins, Vesicular Transport
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 21210912
DOI: 10.1111/j.1600-0854.2011.01159.x

Genes

CPE

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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