Journal
BIOLOGICAL CHEMISTRY
Volume 401, Issue 5, Pages 573-584Publisher
WALTER DE GRUYTER GMBH
DOI: 10.1515/hsz-2019-0375
Keywords
Arf-like protein 3 (ARL3); lipidated proteins; mouse rod and cone photoreceptors; PDE6D (PDE delta); photoreceptor connecting cilium (transition zone); rhodopsin; uncoordinated protein (UNC119)
Categories
Funding
- NIH [EY08123, EY019298, EY014800-039003]
- Research to Prevent Blindness (RPB
- New York)
- Retina Research Foundation (Alice McPherson, MD), Houston
Ask authors/readers for more resources
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 similar to 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 delta (PDE delta) and uncoordinated protein-119 (UNC119), and the cargo dispensation factor (CDF), Arflike protein 3-guanosine triphosphate (ARL3-GTP). As PDE6 and transducin still reside prominently in the OS of PDEd 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available