PUBLICATION
nev (cyfip2) Is required for retinal lamination and axon guidance in the zebrafish retinotectal system
- Authors
- Pittman, A.J., Gaynes, J.A., and Chien, C.B.
- ID
- ZDB-PUB-100614-35
- Date
- 2010
- Source
- Developmental Biology 344(2): 784-794 (Journal)
- Registered Authors
- Chien, Chi-Bin, Gaynes, John, Pittman, Andrew
- Keywords
- Axon pathfinding, Retinal development, Retinotectal topography, CYFIP2/PIR121, WAVE, FMRP
- MeSH Terms
-
- Animals
- Axons/metabolism
- Axons/physiology*
- Cell Movement/genetics
- Mutation
- Neurogenesis
- Optic Lobe, Nonmammalian/metabolism*
- Retina/metabolism
- Retinal Ganglion Cells/metabolism
- Retinal Ganglion Cells/physiology
- Visual Pathways/metabolism
- Zebrafish/genetics*
- Zebrafish/physiology*
- PubMed
- 20537992 Full text @ Dev. Biol.
Citation
Pittman, A.J., Gaynes, J.A., and Chien, C.B. (2010) nev (cyfip2) Is required for retinal lamination and axon guidance in the zebrafish retinotectal system. Developmental Biology. 344(2):784-794.
Abstract
In the zebrafish retinotectal system, retinal ganglion cells (RGCs) project topographically along anterior-posterior (A-P) and dorsal-ventral (D-V) axes to innervate their primary target, the optic tectum. In the nevermind (nev) mutant, D-V positional information is not maintained by dorsonasal retinal axons as they project through the optic tract to the tectum. Here we present a detailed phenotypic analysis of the retinotectal projection in nev and show that dorsonasal axons do eventually find their correct location on the tectum, albeit after taking a circuitous path. Interestingly, nev seems to be specifically required for retinal axons but not for several non-retinal axon tracts. In addition, we find that nev is required both cell autonomously and cell nonautonomously for proper lamination of the retina. We show that nev encodes Cyfip2 (Cytoplasmic FMRP interacting protein 2) and is thus the first known mutation in a vertebrate Cyfip family member. Finally, we show that CYFIP2 acts cell-autonomously in the D-V sorting of dorsonasal RGC axons in the optic tract. CYFIP2 is a highly-conserved protein that lacks known domains or structural motifs but has been shown to interact with Rac and the fragile-X mental retardation protein, suggesting intriguing links to cytoskeletal dynamics and RNA regulation.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping