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Licensed Unlicensed Requires Authentication Published by De Gruyter December 7, 2019

Diffuse or hitch a ride: how photoreceptor lipidated proteins get from here to there

  • Jeanne M. Frederick , Christin Hanke-Gogokhia , Guoxin Ying and Wolfgang Baehr ORCID logo EMAIL logo
From the journal Biological Chemistry

Abstract

Photoreceptors are polarized neurons, with specific subcellular compartmentalization and unique requirements for protein expression and trafficking. Each photoreceptor contains an outer segment (OS) where vision begins, an inner segment (IS) where protein synthesis occurs and a synaptic terminal for signal transmission to second-order neurons. The OS is a large, modified primary cilium attached to the IS by a slender connecting cilium (CC), the equivalent of the transition zone (TZ). Daily renewal of ~10% of the OS requires massive protein biosynthesis in the IS with reliable transport and targeting pathways. Transport of lipidated (‘sticky’) proteins depends on solubilization factors, phosphodiesterase δ (PDEδ) and uncoordinated protein-119 (UNC119), and the cargo dispensation factor (CDF), Arf-like protein 3-guanosine triphosphate (ARL3-GTP). As PDE6 and transducin still reside prominently in the OS of PDEδ and UNC119 germline knockout mice, respectively, we propose the existence of an alternate trafficking pathway, whereby lipidated proteins migrate in rhodopsin-containing vesicles of the secretory pathway.

Acknowledgments

This work was supported in part by NIH grants EY08123, EY019298 (WB; EY014800-039003 (NEI core grant), Funder Id: http://dx.doi.org/10.13039/100000053; unrestricted grants to the University of Utah Department of Ophthalmology from Research to Prevent Blindness (RPB; New York). W.B. is the recipient of an RPB Senior Investigator award, a RPB Nelson Trust Award, and an award from the Retina Research Foundation (Alice McPherson, MD), Houston.

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Received: 2019-09-20
Accepted: 2019-12-02
Published Online: 2019-12-07
Published in Print: 2020-04-28

©2020 Walter de Gruyter GmbH, Berlin/Boston

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