PUBLICATION
Zebrafish Prickle1b mediates facial branchiomotor neuron migration via a farnesylation-dependent nuclear activity
- Authors
- Mapp, O.M., Walsh, G.S., Moens, C.B., Tada, M., and Prince, V.E.
- ID
- ZDB-PUB-110518-43
- Date
- 2011
- Source
- Development (Cambridge, England) 138(10): 2121-2132 (Journal)
- Registered Authors
- Mapp, Oni, Moens, Cecilia, Prince, Victoria E., Tada, Masazumi, Walsh, Gregory
- Keywords
- facial branchiomotor neurons, Prickle1b, neuronal migration, REST, farnesylation, zebrafish
- MeSH Terms
-
- Zebrafish Proteins/antagonists & inhibitors
- Zebrafish Proteins/genetics
- Zebrafish Proteins/metabolism*
- Animals, Genetically Modified
- Models, Biological
- Mutation
- Hydroxymethylglutaryl CoA Reductases/metabolism
- Farnesyltranstransferase/metabolism
- Neurogenesis
- Gene Expression Regulation, Developmental
- Repressor Proteins/genetics
- Repressor Proteins/metabolism
- Gene Knockdown Techniques
- Animals
- DNA, Complementary/genetics
- Zebrafish/embryology*
- Zebrafish/genetics
- Zebrafish/metabolism*
- LIM Domain Proteins
- Sequence Homology, Amino Acid
- Carrier Proteins/antagonists & inhibitors
- Carrier Proteins/genetics
- Carrier Proteins/metabolism*
- Amino Acid Sequence
- Molecular Sequence Data
- Motor Neurons/cytology
- Motor Neurons/metabolism
- Signal Transduction
- Protein Prenylation
- Adaptor Proteins, Signal Transducing
- Cell Nucleus/metabolism
- Cell Movement
- Base Sequence
- PubMed
- 21521740 Full text @ Development
Citation
Mapp, O.M., Walsh, G.S., Moens, C.B., Tada, M., and Prince, V.E. (2011) Zebrafish Prickle1b mediates facial branchiomotor neuron migration via a farnesylation-dependent nuclear activity. Development (Cambridge, England). 138(10):2121-2132.
Abstract
The facial branchiomotor neurons (FBMNs) undergo a characteristic tangential migration in the vertebrate hindbrain. We previously used a morpholino knockdown approach to reveal that zebrafish prickle1b (pk1b) is required for this migration. Here we report that FBMN migration is also blocked in a pk1b mutant with a disruption in the consensus farnesylation motif. We confirmed that this lipid modification is required during FBMN migration by disrupting the function of farnesyl biosynthetic enzymes. Furthermore, farnesylation of a tagged Pk1b is required for its nuclear localization. Using a unique rescue approach, we have demonstrated that Pk1b nuclear localization and farnesylation are required during FBMN migration. Our data suggest that Pk1b acts at least partially independently of core planar cell polarity molecules at the plasma membrane, and might instead be acting at the nucleus. We also found that the neuronal transcriptional silencer REST is necessary for FBMN migration, and we provide evidence that interaction between Pk1b and REST is required during this process. Finally, we demonstrate that REST protein, which is normally localized in the nuclei of migrating FBMNs, is depleted from the nuclei of Pk1b-deficient neurons. We conclude that farnesylation-dependent nuclear localization of Pk1b is required to regulate REST localization and thus FBMN migration.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping