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The EGL-21 Carboxypeptidase E Facilitates Acetylcholine Release at Caenorhabditis elegans Neuromuscular Junctions

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Jacob, Tija C., Kaplan, Joshua M .·2003·The Journal of Neuroscience

Abstract

Proneuropeptides are packaged into dense-core vesicles in which they are processed into active peptides by copackaged enzymes. Proprotein convertases (PCs) cleave precursors after dibasic residues, and carboxypeptidases remove basic residues from the C terminals. We show here that the Caenorhabditis elegans egl-21 gene encodes a protein that is very similar to carboxypeptidase E (CPE) and is broadly expressed in the nervous system. Mutants lacking either egl-21 CPE or egl-3, which encodes the C. elegans ortholog of PC type 2 (PC2), were defective for processing endogenously expressed FMRFamide (Phe-Met-Arg-Phe-NH2)-related peptides (FaRPs). Mutants lacking the unc-104 kinesin motor protein were defective for anterograde movement of dense-core vesicle components, including egl-3 PC2,egl-21 CPE, and FaRPs. We provide evidence that egl-3 PC2 and egl-21 CPE mutants have diminished acetylcholine release at neuromuscular junctions (NMJs). Taken together, these results suggest that egl-21 CPE and egl-3 PC2 process endogenous neuropeptides that facilitate acetylcholine release at C. elegans NMJs.

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Metadata

Authors
Jacob, T. C., & Kaplan, J. M.
Venue
The Journal of Neuroscience
Published
2003-03-15
Volume
23
Issue
6
Pages
2122-2130
ISSN
  • 0270-6474 (ISSN-L)
  • 1529-2401
OpenAlex
W2143225227
Cited by
163
References
0
FWCI
2.11
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: The EGL-21 Carboxypeptidase E Facilitates Acetylcholine Release at Caenorhabditis elegans Neuromuscular Junctions. https://app.cochat.ai/papers/10.1523/jneurosci.23-06-02122.2003
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Jacob, T. C., & Kaplan, J. M. (2003). The EGL-21 Carboxypeptidase E Facilitates Acetylcholine Release at Caenorhabditis elegans Neuromuscular Junctions. The Journal of Neuroscience. https://doi.org/10.1523/jneurosci.23-06-02122.2003

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