Classes of non-conventional tetraspanins defined by alternative splicing

Tetraspanins emerge as a family of membrane proteins mediating an exceptional broad diversity of functions. The naming refers to their four transmembrane segments, which define the tetraspanins‘ typical membrane topology. In this study, we analyzed alternative splicing of tetraspanins. Besides isofo...

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Bibliographic Details
Published in:Scientific reports 2019-10, Vol.9 (1), p.14075-13, Article 14075
Main Authors: Hochheimer, Nikolas, Sies, Ricarda, Aschenbrenner, Anna C., Schneider, Dirk, Lang, Thorsten
Format: Article
Language:English
Subjects:
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Alternative Splicing
Biochemistry
Endoplasmic Reticulum - metabolism
Genes
Genomes
Genomics
Humanities and Social Sciences
Humans
Isoforms
Isomerism
Membrane proteins
Membrane Proteins - chemistry
Membrane Proteins - metabolism
mRNA
multidisciplinary
Names
Proteins
Proteomics
Science
Science (multidisciplinary)
Structure-Activity Relationship
Tetraspanins - chemistry
Tetraspanins - metabolism
Topology
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Summary:Tetraspanins emerge as a family of membrane proteins mediating an exceptional broad diversity of functions. The naming refers to their four transmembrane segments, which define the tetraspanins‘ typical membrane topology. In this study, we analyzed alternative splicing of tetraspanins. Besides isoforms with four transmembrane segments, most mRNA sequences are coding for isoforms with one, two or three transmembrane segments, representing structurally mono-, di- and trispanins. Moreover, alternative splicing may alter transmembrane topology, delete parts of the large extracellular loop, or generate alternative N- or C-termini. As a result, we define structure-based classes of non-conventional tetraspanins. The increase in gene products by alternative splicing is associated with an unexpected high structural variability of tetraspanins. We speculate that non-conventional tetraspanins have roles in regulating ER exit and modulating tetraspanin-enriched microdomain function.
ISSN:2045-2322
2045-2322
DOI:10.1038/s41598-019-50267-0