# CPD-1 can compensate for EGL-21 to process neuropeptides

**Authors:** David C Khawand, Amy K Clippinger, Michael Ailion

PMC · DOI: 10.17912/micropub.biology.001965 · microPublication Biology · 2026-01-06

## TL;DR

This study shows that CPD-1 can help process neuropeptides when another enzyme, EGL-21, is missing, affecting defecation in C. elegans.

## Contribution

The novel finding is that CPD-1 compensates for EGL-21 in neuropeptide processing, specifically in C. elegans defecation.

## Key findings

- cpd-1 mutants alone do not cause defecation defects.
- cpd-1 enhances defecation defects in egl-21 mutants.
- CPD-1 acts in intestinal cells and possibly GABAergic neurons.

## Abstract

Carboxypeptidase D has been thought to process neuropeptides, though its role has not been fully characterized. Since specific neuropeptides regulate the defecation motor program of

C. elegans

, we used genetic analysis to determine how loss of the worm carboxypeptidase D ortholog
CPD-1
affects defecation. We found that

cpd-1

mutants do not have defecation defects but enhance the defecation defects of

egl-21

mutants lacking carboxypeptidase E, a major neuropeptide processing enzyme. We also found that
CPD-1
acts in intestinal cells and possibly GABAergic neurons to promote defecation. These results suggest that
CPD-1
can process neuropeptides, specifically in the absence of
EGL-21
.

## Linked entities

- **Genes:** CLA3 (cerebellar ataxia 3 (cerebellar parenchyma disorder 1)) [NCBI Gene 1167], egl-21 (Carboxypeptidase E) [NCBI Gene 177940]

## Full-text entities

- **Genes:** egl-21 (Carboxypeptidase E) [NCBI Gene 177940], cpd-1 (Peptidase M14 domain-containing protein) [NCBI Gene 172206]
- **Species:** C. elegans [taxon 328850]

## Full text

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## Figures

1 figure with captions in the complete paper: https://tomesphere.com/paper/PMC12820724/full.md

## References

15 references — full list in the complete paper: https://tomesphere.com/paper/PMC12820724/full.md

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Source: https://tomesphere.com/paper/PMC12820724