PUBLICATION
Zebrafish fat-free is required for intestinal lipid absorption and Golgi apparatus structure
- Authors
- Ho, S.Y., Lorent, K., Pack, M., and Farber, S.A.
- ID
- ZDB-PUB-060412-3
- Date
- 2006
- Source
- Cell Metabolism 3(4): 289-300 (Journal)
- Registered Authors
- Farber, Steven, Ho, Shiu-Ying, Lorent, Kristin, Pack, Michael
- Keywords
- none
- MeSH Terms
-
- Microscopy, Confocal
- Enterocytes/chemistry
- Enterocytes/physiology
- Lipid Metabolism*
- Transport Vesicles
- Endosomes/physiology
- Protein Structure, Tertiary
- Fluorescent Antibody Technique
- Humans
- Membrane Proteins/genetics
- Membrane Proteins/physiology
- Amino Acid Sequence
- Animals
- Male
- Protein Transport
- Mutation
- Zebrafish
- Vesicular Transport Proteins/chemistry
- Vesicular Transport Proteins/genetics*
- Vesicular Transport Proteins/physiology*
- Gene Expression Regulation
- Phenotype
- Golgi Apparatus/chemistry
- Golgi Apparatus/ultrastructure*
- Molecular Sequence Data
- Recombinant Fusion Proteins/metabolism
- Zebrafish Proteins/chemistry
- Zebrafish Proteins/genetics*
- Zebrafish Proteins/physiology*
- Intestinal Absorption*
- PubMed
- 16581006 Full text @ Cell Metab.
Citation
Ho, S.Y., Lorent, K., Pack, M., and Farber, S.A. (2006) Zebrafish fat-free is required for intestinal lipid absorption and Golgi apparatus structure. Cell Metabolism. 3(4):289-300.
Abstract
The zebrafish fat-free (ffr) mutation was identified in a physiological screen for genes that regulate lipid metabolism. ffr mutant larvae are morphologically indistinguishable from wild-type sibling larvae, but their absorption of fluorescent lipids is severely impaired. Through positional cloning, we have identified a causative mutation in a highly conserved and ubiquitously expressed gene within the ffr locus. The Ffr protein contains a Dor-1 like domain typical of oligomeric Golgi complex (COG) gene, cog8. Golgi complex ultrastructure is disrupted in the ffr digestive tract. Consistent with a possible role in COG-mediated Golgi function, wild-type Ffr-GFP and COG8-mRFP fusion proteins partially colocalize in zebrafish blastomeres. Enterocyte retention of an endosomal lipid marker in ffr larvae support the idea that altered vesicle trafficking contributes to the ffr mutant defect. These data indicate that ffr is required for both Golgi structure and vesicular trafficking, and ultimately lipid transport.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping