Extraocular, rod-like photoreceptors in a flatworm express xenopsin photopigment

Kate a Rawlinson; Francois Lapraz; Edward r Ballister; Mark Terasaki; Jessica Rodgers; Richard j Mcdowell; Johannes Girstmair; Katharine e Criswell; Miklos Boldogkoi; Fraser Simpson; David Goulding; Claire Cormie; Brian Hall; Robert j Lucas; Maximilian j Telford

doi:10.7554/eLife.45465

Extraocular, rod-like photoreceptors in a flatworm express xenopsin photopigment

Kate a Rawlinson, Francois Lapraz, Edward r Ballister, Mark Terasaki, Jessica Rodgers, Richard j Mcdowell, Johannes Girstmair, Katharine e Criswell, Miklos Boldogkoi, Fraser Simpson, David Goulding, Claire Cormie, Brian Hall, Robert j Lucas, Maximilian j Telford

Research output: Contribution to journal › Article › peer-review

Abstract

Animals detect light using opsin photopigments. Xenopsin, a recently classified subtype of opsin, challenges our views on opsin and photoreceptor evolution. Originally thought to belong to the Gαi-coupled ciliary opsins, xenopsins are now understood to have diverged from ciliary opsins in pre-bilaterian times, but little is known about the cells that deploy these proteins, or if they form a photopigment and drive phototransduction. We characterized xenopsin in a flatworm, Maritigrella crozieri, and found it expressed in ciliary cells of eyes in the larva, and in extraocular cells around the brain in the adult. These extraocular cells house hundreds of cilia in an intra-cellular vacuole (phaosome). Functional assays in human cells show Maritigrella xenopsin drives phototransduction primarily by coupling to Gαi. These findings highlight similarities between xenopsin and c-opsin and reveal a novel type of opsin-expressing cell that, like jawed vertebrate rods, encloses the ciliary membrane within their own plasma membrane.

Original language	English
Pages (from-to)	e45465
Journal	eLife
Volume	8
DOIs	https://doi.org/10.7554/eLife.45465
Publication status	Published - 30 Oct 2019

Keywords

Opsin
GPCR
Xenopsin
Evolution

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10.7554/eLife.45465

https://elifesciences.org/articles/45465

Centre for Biological Timing
Lucas, R. (PI), Bechtold, D. (PI), Fustin, J.-M. (PI), Ashe, H. (PI), Brown, T. (PI), Blaikley, J. (PI), Brass, A. (PI), Chandola, T. (PI), Durrington, H. (PI), Else, K. (PI), Hepworth, M. (PI), Hunter, L. (PI), Kadler, K. (PI), Kitchen, G. (PI), Loudon, A. (PI), Macdonald, A. (PI), Mcbeth, J. (PI), Milosavljevic, N. (PI), Rattray, M. (PI), Rutter, M. (PI), Sharrocks, A. (PI), Spiller, D. (PI), Storchi, R. (PI), Belle, M. (PI), Meng, Q.-J. (PI), Allen, A. (PI), Dixon, W. (PI), Gibbs, J. (PI), Hazel, A. (PI), Papalopulu, N. (PI), Ray, D. (PI), White, M. (PI) & Chang, J. (PI)
Project: Research

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title = "Extraocular, rod-like photoreceptors in a flatworm express xenopsin photopigment",

abstract = "Animals detect light using opsin photopigments. Xenopsin, a recently classified subtype of opsin, challenges our views on opsin and photoreceptor evolution. Originally thought to belong to the Gαi-coupled ciliary opsins, xenopsins are now understood to have diverged from ciliary opsins in pre-bilaterian times, but little is known about the cells that deploy these proteins, or if they form a photopigment and drive phototransduction. We characterized xenopsin in a flatworm, Maritigrella crozieri, and found it expressed in ciliary cells of eyes in the larva, and in extraocular cells around the brain in the adult. These extraocular cells house hundreds of cilia in an intra-cellular vacuole (phaosome). Functional assays in human cells show Maritigrella xenopsin drives phototransduction primarily by coupling to Gαi. These findings highlight similarities between xenopsin and c-opsin and reveal a novel type of opsin-expressing cell that, like jawed vertebrate rods, encloses the ciliary membrane within their own plasma membrane.",

keywords = "Opsin, GPCR, Xenopsin, Evolution",

author = "Rawlinson, {Kate a} and Francois Lapraz and Ballister, {Edward r} and Mark Terasaki and Jessica Rodgers and Mcdowell, {Richard j} and Johannes Girstmair and Criswell, {Katharine e} and Miklos Boldogkoi and Fraser Simpson and David Goulding and Claire Cormie and Brian Hall and Lucas, {Robert j} and Telford, {Maximilian j}",

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doi = "10.7554/eLife.45465",

language = "English",

volume = "8",

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AU - Rawlinson, Kate a

AU - Lapraz, Francois

AU - Ballister, Edward r

AU - Terasaki, Mark

AU - Rodgers, Jessica

AU - Mcdowell, Richard j

AU - Girstmair, Johannes

AU - Criswell, Katharine e

AU - Boldogkoi, Miklos

AU - Simpson, Fraser

AU - Goulding, David

AU - Cormie, Claire

AU - Hall, Brian

AU - Lucas, Robert j

AU - Telford, Maximilian j

PY - 2019/10/30

Y1 - 2019/10/30

N2 - Animals detect light using opsin photopigments. Xenopsin, a recently classified subtype of opsin, challenges our views on opsin and photoreceptor evolution. Originally thought to belong to the Gαi-coupled ciliary opsins, xenopsins are now understood to have diverged from ciliary opsins in pre-bilaterian times, but little is known about the cells that deploy these proteins, or if they form a photopigment and drive phototransduction. We characterized xenopsin in a flatworm, Maritigrella crozieri, and found it expressed in ciliary cells of eyes in the larva, and in extraocular cells around the brain in the adult. These extraocular cells house hundreds of cilia in an intra-cellular vacuole (phaosome). Functional assays in human cells show Maritigrella xenopsin drives phototransduction primarily by coupling to Gαi. These findings highlight similarities between xenopsin and c-opsin and reveal a novel type of opsin-expressing cell that, like jawed vertebrate rods, encloses the ciliary membrane within their own plasma membrane.

AB - Animals detect light using opsin photopigments. Xenopsin, a recently classified subtype of opsin, challenges our views on opsin and photoreceptor evolution. Originally thought to belong to the Gαi-coupled ciliary opsins, xenopsins are now understood to have diverged from ciliary opsins in pre-bilaterian times, but little is known about the cells that deploy these proteins, or if they form a photopigment and drive phototransduction. We characterized xenopsin in a flatworm, Maritigrella crozieri, and found it expressed in ciliary cells of eyes in the larva, and in extraocular cells around the brain in the adult. These extraocular cells house hundreds of cilia in an intra-cellular vacuole (phaosome). Functional assays in human cells show Maritigrella xenopsin drives phototransduction primarily by coupling to Gαi. These findings highlight similarities between xenopsin and c-opsin and reveal a novel type of opsin-expressing cell that, like jawed vertebrate rods, encloses the ciliary membrane within their own plasma membrane.

KW - Opsin

KW - GPCR

KW - Xenopsin

KW - Evolution

U2 - 10.7554/eLife.45465

DO - 10.7554/eLife.45465

M3 - Article

SN - 2050-084X

VL - 8

SP - e45465

JO - eLife

JF - eLife

ER -

Extraocular, rod-like photoreceptors in a flatworm express xenopsin photopigment

Abstract

Keywords

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