Evidence map›Paper›PMID 26787743›Full record

ArticleJournal of cell science2016

Early eukaryotic origins for cilia-associated bioactive peptide-amidating activity.

Dhivya Kumar, Crysten E Blaby-Haas, Sabeeha S Merchant, Richard E Mains, Stephen M King, Betty A Eipper

Abstract read
In one paragraph

Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.7field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. Germline loss-of-functionmedRxiv : the preprint server for health sciences · 2023
    Article
  3. Germline loss-of-functionFrontiers in endocrinology · 2023
    Article
  4. Review
  5. Regulated processing and secretion of a peptide precursor in cilia.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Review
  7. Premetazoan Origin of Neuropeptide Signaling.Molecular biology and evolution · 2022
    Article
  8. Towards the Idea of Molecular Brains.International journal of molecular sciences · 2021
    Review
  9. The chemical brain hypothesis for the origin of nervous systems.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2021
    Article
  10. Article
  11. From economy to luxury: Copper homeostasis in Chlamydomonas and other algae.Biochimica et biophysica acta. Molecular cell research · 2020
    Review
  12. Article
  13. Review
  14. Proteases Shape theProteomes · 2018
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Dhivya KumarDepartment of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 06030-3401, USA.
Crysten E Blaby-HaasDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095-1569, USA.
Sabeeha S MerchantDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095-1569, USA Institute for Genomics and Proteomics, University of California, Los Angeles, CA 90095-1569, USA.
Richard E MainsDepartment of Neuroscience, University of Connecticut Health Center, Farmington, CT 06030-3401, USA.
Stephen M KingDepartment of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 06030-3401, USA eipper@uchc.edu sking@uchc.edu.
Betty A EipperDepartment of Molecular Biology and Biophysics, University of Connecticut Health Center, Farmington, CT 06030-3401, USA Department of Neuroscience, University of Connecticut Health Center, Farmington, CT 06030-3401, USA eipper@uchc.edu sking@uchc.edu.
UConn Health · USUniversity of California, Los Angeles · US

Funding

MOLECULAR ANALYSIS OF FLAGELLAR DYNEIN FUNCTIONR01GM051293 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI KING, STEPHEN M · 1995 to 2020
$6.9M
BIOCHEMISTRY AND PHYSIOLOGY OF PEPTIDE AMIDATIONR01DK032949 · NIDDK · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI EIPPER, ELIZABETH ANNE, KING, STEPHEN M · 1986 to 2017
$6.4M
Nutritional Cu Signaling and HomeostasisR01GM042143 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SABEEHA MERCHANT · 1995 to 2026
$4.6M
Nutritional Copper Signaling and HomeostasisR37GM042143 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MERCHANT, SABEEHA · 2011 to 2020
$4.3M
BIOCHEMISTRY AND PHYSIOLOGY OF PEPTIDE AMIDATIONR37DK032949 · NIDDK · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI EIPPER, ELIZABETH A · 1989 to 2004
$2.8M
Dissection of the Molecular Details of Fe Deficiency AcclimationF32GM100753 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BLABY, CRYSTEN ELIZABETH · 2012 to 2014
$156k
BIOCHEMISTRY AND PHYSIOLOGY OF PEPTIDE AMIDATIONR56DK032949 · NIDDK · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI EIPPER, ELIZABETH A · 2005 to 2005
$104k
CU-DEPENDENT TRANSCRIPTIONAL REGULATIONR29GM042143 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MERCHANT, SABEEHA · 1989 to 1993
–
NIDDK NIH HHS DK032949NIDDK NIH HHS R01 DK032949NIDDK NIH HHS R37 DK032949NIDDK NIH HHS R56 DK032949NIGMS NIH HHS F32 GM100753NIGMS NIH HHS GM042143NIGMS NIH HHS GM051293NIGMS NIH HHS GM100753NIGMS NIH HHS R01 GM042143NIGMS NIH HHS R01 GM051293NIGMS NIH HHS R37 GM042143
6 · The paper itself

Abstract

Ciliary axonemes and basal bodies were present in the last eukaryotic common ancestor and play crucial roles in sensing and responding to environmental cues. Peptidergic signaling, generally considered a metazoan innovation, is essential for organismal development and homeostasis. Peptidylglycine α-amidating monooxygenase (PAM) is crucial for the last step of bioactive peptide biosynthesis. However, identification of a complete PAM-like gene in green algal genomes suggests ancient evolutionary roots for bioactive peptide signaling. We demonstrate that the Chlamydomonas reinhardtii PAM gene encodes an active peptide-amidating enzyme (CrPAM) that shares key structural and functional features with the mammalian enzyme, indicating that components of the peptide biosynthetic pathway predate multicellularity. In addition to its secretory pathway localization, CrPAM localizes to cilia and tightly associates with the axonemal superstructure, revealing a new axonemal enzyme activity. This localization pattern is conserved in mammals, with PAM present in both motile and immotile sensory cilia. The conserved ciliary localization of PAM adds to the known signaling capabilities of the eukaryotic cilium and provides a potential mechanistic link between peptidergic signaling and endocrine abnormalities commonly observed in ciliopathies.

Indexed as

AnimalsChlamydomonas reinhardtiiCiliaEvolution, MolecularHEK293 CellsHumansMiceNIH 3T3 CellsNitrogenous Group TransferasesPlant ProteinsProtein Processing, Post-TranslationalProtein TransportNitrogenous Group TransferasesPlant ProteinsAmidationAxonemeChlamydomonasCuproenzymeMonooxygenaseNeuropeptide

Identifiers

PMID26787743
PMCPMC4813317
OpenAlexW2298520537

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.