Evidence map›Paper›PMID 38668976›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2024

Gap Junctions in Ctenophora.

Andrea B Kohn, Leonid L Moroz

Abstract read
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Article in Methods in molecular biology (Clifton, N.J.), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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5 · Who and what money

Authors and funding

2 authors.

Andrea B KohnWhitney Laboratory for Marine Bioscience, University of Florida, St. Augustine, FL, USA.
Leonid L MorozWhitney Laboratory for Marine Bioscience, University of Florida, St. Augustine, FL, USA. moroz@whitney.ufl.edu.

Funding

Neuron-SELEX: Development of neuron-specific nanoscale toolkits for single-cell recognitionR01NS114491 · NINDS · UNIVERSITY OF FLORIDA · PI MOROZ, LEONID L · 2020 to 2024
$2.0M
NINDS NIH HHS R01 NS114491
6 · The paper itself

Abstract

Gap junction proteins form specialized intercellular communication channels, including electrical synapses, that regulate cellular metabolism and signaling. We present a molecular inventory of the gap junction proteins-innexins (INX-like) in ctenophores, focusing on two reference species, Pleurobrachia bachei and Mnemiopsis leidyi. Innexins were identified in more than 15 ctenophore species, including such genera as Euplokamis, Pukia, Hormiphora, Bolinopsis, Cestum, Ocyropsis, Dryodora, Beroe, benthic ctenophores, Coeloplana and Vallicula, and undescribed species of Mertensiidae. The observed diversity of innexins resulted from the independent expansion of this family from the common ancestor of ctenophores. Innexins show the conserved topology with four transmembrane domains connected by two extracellular loops, which bridge intracellular gaps. However, INX-like genes have highly diverse exon organization and low percentage identity for their amino acid sequences within the same species and between ctenophore species. Such a broad scope of molecular diversity differs from innexins in other phyla. We predicted posttranslational modifications in innexins: 249 and 188 for M. leidyi and P. bachei, respectively. Neither their number nor their locations were conserved within or between species. When the number of posttranslational modifications is factored into the innexins' radiation, the potential for molecular and physiological diversity within gap junctions of ctenophores is almost unfathomable. RNA-seq and in situ hybridization data revealed that innexins are expressed across embryogenesis, including early cleavage stages and gastrulation. They are abundant in all adult tissues, with the highest expression level in the aboral organ (the major integrative center and the gravity sensor in ctenophores), followed by tentacles and comb plates. Nevertheless, each organ and tissue has a unique combination of innexins, suggesting their involvement in complex integrative functions and behaviors of ctenophores.

Indexed as

CtenophoraGap JunctionsAmino Acid SequenceAnimalsPhylogenyCtenophoraEvolutionInnexinMnemiopsisPannexinPhylogenyPleurobrachiaPosttranslational modifications

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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.