Abstract

Intercellular gap junction channels and single-membrane channels have been reported to regulate electrical synapse and the brain function. Innexin is known as a gap junction-related protein in invertebrates and is involved in the formation of intercellular gap junction channels and single-cell membrane channels. Multiple isoforms of innexin protein in each species enable the precise regulation of channel function. In molluscan species, sequence information of innexins is still limited and the sequences of multiple innexin isoforms have not been classified. This study examined the innexin transcripts expressed in the central nervous system of the terrestrial slug Limax valentianus and identified 16 transcripts of 12 innexin isoforms, including the splicing variants. We performed phylogenetic analysis and classified the isoforms with other molluscan innexin sequences. Next, the phosphorylation, N-glycosylation, and S-nitrosylation sites were predicted to characterize the innexin isoforms. Further, we identified 16 circular RNA sequences of nine innexin isoforms in the central nervous system of Limax. The identification and classification of molluscan innexin isoforms provided novel insights for understanding the regulatory mechanism of innexin in this phylum.

Highlights

  • Gap junction channels are formed by docking of single-cell membrane channels between adjacent cells, and that allow intercellular communication via the exchange of small molecules such as ions, nucleotides, small peptides, and micro RNA

  • To identify the gene transcripts of gap junction proteins in the Limax central nervous system (CNS), a local BLASTX search was performed for our transcriptome data using sequences of Aplysia innexin homologs

  • We identified 16 Limax innexin homologs with the entire coding domain sequence (CDS) (Limax innexin 1–11 including spliced isoforms) and partial CDS of Limax innexin 12

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Summary

Introduction

Gap junction channels are formed by docking of single-cell membrane channels between adjacent cells, and that allow intercellular communication via the exchange of small molecules such as ions, nucleotides, small peptides, and micro RNA (miRNA). Previous studies have indicated that the gap junction-related proteins are involved in the regulation of brain function. Neuronal gap junctions work as electrical synapses and exhibit plasticity [1, 2]. Single-cell membrane channels, which do not form intercellular channels, are involved in neuroplasticity through their interaction with chemical synapses [2, 3]. The channel properties of gap junction-related proteins are regulated by protein modifications such as N-glycosylation, S-nitrosylation, and phosphorylation [4,5,6,7].

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