Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Identification of a novel prohormone sorting signal-binding site on carboxypeptidase E, a regulated secretory pathway-sorting receptor.

Molecular endocrinology (Baltimore, Md.) - 1 Apr 1999

Zhang C F, Snell C R, Loh Y P

Abstract excerpt

Sorting of the prohormone POMC to the regulated secretory pathway necessitates the binding of a sorting signal to a sorting receptor, identified as membrane carboxypeptidase E (CPE). The sorting signal, located at the N terminus of POMC consists of two acidic (Asp10, Glu14) and two hydrophobic (Leu11, Leu18) residues exposed on the surface of an amphipathic loop. In this study, molecular modeling of CPE predicted...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Baculoviridae
Share to Carboxypeptidases
Share to Enkephalins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Insecta

Share to Lysine

Share to Pro-Opiomelanocortin

Share to Proinsulin

Share to Protein Precursors

Source

Identifiers

PMID: 10194759
DOI: 10.1210/mend.13.4.0267

Genes

CPE
POMC

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.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of a novel prohormone sorting signal-binding site on carboxypeptidase E, a regulated secretory pathway-sorting receptor.PMID 10194759Read ↗

Disruption of a receptor-mediated mechanism for intracellular sorting of proinsulin in familial hyperproinsulinemia.Semantic proximity Read ↗

Secretory granule biogenesis and neuropeptide sorting to the regulated secretory pathway in neuroendocrine cells.Semantic proximity Read ↗

Luminal interaction of phogrin with carboxypeptidase E for effective targeting to secretory granules.Semantic proximity Read ↗

Recycling of Raft-associated prohormone sorting receptor carboxypeptidase E requires interaction with ARF6.Semantic proximity Read ↗

Mutations in the amino-terminal region of proopiomelanocortin (POMC) in patients with early-onset obesity impair POMC sorting to the regulated secretory pathway.Semantic proximity Read ↗

Targeting of pro-opiomelanocortin to the regulated secretory pathway may involve cooperation between different protein domains.Semantic proximity Read ↗

Cell surface targeting of the Melanocortin 5 Receptor (MC5R) requires serine-rich terminal motifs.Semantic proximity Read ↗

Hypothalamic proopiomelanocortin processing and the regulation of energy balance.Semantic proximity Read ↗

A prohormone convertase cleavage site within a predicted alpha-helix mediates sorting of the neuronal and endocrine polypeptide VGF into the regulated secretory pathway.Semantic proximity Read ↗

Processing and trafficking of a prohormone convertase 2 active site mutant.Semantic proximity Read ↗

Sorting and activity-dependent secretion of BDNF require interaction of a specific motif with the sorting receptor carboxypeptidase e.Semantic proximity Read ↗

COP-binding sites in p24delta2 are necessary for proper secretory cargo biosynthesis.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.