ArticleJournal of molecular evolution2008
Type II opsins: evolutionary origin by internal domain duplication?
Article in Journal of molecular evolution, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 38 citations in OpenAlex.
- Convergent evolution of animal and microbial rhodopsins.RSC advances · 2023Review
- Pseudo-Symmetric Assembly of Protodomains as a Common Denominator in the Evolution of Polytopic Helical Membrane Proteins.Journal of molecular evolution · 2020Article
- The awesome power of optogenetics in hearing research.Neuroscience letters · 2019Review
- A Large and Phylogenetically Diverse Class of Type 1 Opsins Lacking a Canonical Retinal Binding Site.PloS one · 2016Article
- An empirical test of convergent evolution in rhodopsins.Molecular biology and evolution · 2014Article
- Relocating the active-site lysine in rhodopsin and implications for evolution of retinylidene proteins.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Evidence from Chlamydomonas on the photoactivation of rhodopsins without isomerization of their chromophore.Chemistry & biology · 2011Article
- The evolution of phototransduction from an ancestral cyclic nucleotide gated pathway.Proceedings. Biological sciences · 2010Article
- The predictability of evolution: glimpses into a post-Darwinian world.Die Naturwissenschaften · 2009Review
- The evolution of eyes and visually guided behaviour.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2009Review
- Eye evolution: common use and independent recruitment of genetic components.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2009Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Opsins are a large group of proteins with seven transmembrane segments (TMSs) that are found in all domains of life. There are two types of opsins that are sometimes considered nonhomologous: type I is known from prokaryotes and some eukaryotes, while type II is known only from Eumetazoan animals. Type II opsins are members of the family of G-protein coupled receptors (GPCRs), which facilitate signal transduction across cell membranes. While previous studies have concluded that multiple transmembrane-containing protein families-including type I opsins-originated by internal domain duplication, the origin of type II opsins has been speculated on but never tested. Here we show that type II opsins do not appear to have originated through a similar internal domain duplication event. This provides further evidence that the two types of opsins are nonhomologous, indicating a convergent evolutionary origin, in which both groups of opsins evolved a seven-TM structure and light sensitivity independently. This convergence may indicate an important role for seven-TM protein structure for retinal-based light sensitivity.
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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.