PUBLICATION
Eomesodermin requires TGF-beta /activin signaling and binds Smad2 to activate mesodermal genes
- Authors
- Picozzi, P., Wang, F., Cronk, K., and Ryan, K.
- ID
- ZDB-PUB-081203-24
- Date
- 2009
- Source
- The Journal of biological chemistry 284(4): 2397-2408 (Journal)
- Registered Authors
- Keywords
- none
- MeSH Terms
-
- Activins/metabolism*
- Amino Acid Sequence
- Animals
- Antibodies/immunology
- Binding Sites
- Cell Membrane/metabolism
- Gene Expression Regulation, Developmental
- Humans
- Mesoderm/embryology
- Mesoderm/metabolism
- Molecular Sequence Data
- Protein Binding
- Sepharose/metabolism
- Sequence Alignment
- Signal Transduction*
- Smad2 Protein/genetics
- Smad2 Protein/metabolism*
- T-Box Domain Proteins/chemistry
- T-Box Domain Proteins/genetics
- T-Box Domain Proteins/immunology
- T-Box Domain Proteins/metabolism*
- Transforming Growth Factor beta/metabolism*
- Xenopus Proteins/chemistry
- Xenopus Proteins/genetics
- Xenopus Proteins/immunology
- Xenopus Proteins/metabolism*
- Xenopus laevis/embryology
- Xenopus laevis/genetics
- Xenopus laevis/metabolism
- PubMed
- 19036723 Full text @ J. Biol. Chem.
Citation
Picozzi, P., Wang, F., Cronk, K., and Ryan, K. (2009) Eomesodermin requires TGF-beta /activin signaling and binds Smad2 to activate mesodermal genes. The Journal of biological chemistry. 284(4):2397-2408.
Abstract
The T-box gene Eomesodermin (Eomes) is required for early embryonic mesoderm differentiation in mouse, frog (Xenopus laevis), and zebrafish, is important in late cardiac development in Xenopus, and for CD8+ T effector cell function in mouse. Eomes can ectopically activate many mesodermal genes. However, the mechanism by which Eomes activates transcription of these genes is poorly understood. We report that Eomes protein interacts with Smad2 and is capable of working in a non cell autonomous manner via transfer of Eomes protein between adjacent embryonic cells. Blocking of Eomes protein transfer using a farnesylated red fluorescent protein (CherryF) also prevents Eomes nuclear accumulation. Transfer of Eomes protein between cells is mediated by the Eomes carboxyl terminus (456-692). A carbohydrate binding domain within the Eomes carboxyl terminal region is sufficient for transfer and important for gene activation. We propose a novel mechanism by which Eomes helps effect a cellular response to a morphogen gradient.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping