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Reference
Citation
Comer, A.R., Ahern-Djamali, S.M., Juang, J.L., Jackson, P.D., Hoffmann, F.M. (1998). Phosphorylation of Enabled by the Drosophila Abelson tyrosine kinase regulates the in vivo function and protein-protein interactions of Enabled.  Mol. Cell. Biol. 18(1): 152--160.
FlyBase ID
FBrf0099996
Publication Type
Research paper
Abstract

Drosophila Enabled (Ena) is a member of a family of cytoskeleton-associated proteins including mammalian vasodilator-stimulated phosphoprotein and murine Enabled that regulate actin cytoskeleton assembly. Mutations in Drosophila ena were discovered as dominant genetic suppressors of mutations in the Abelson tyrosine kinase (Abl), suggesting that Ena and Abl function in the same pathway or process. We have identified six tyrosine residues on Ena that are phosphorylated by Abl in vitro and in vivo. Mutation of these phosphorylation sites to phenylalanine partially impaired the ability of Ena to restore viability to ena mutant animals, indicating that phosphorylation is required for optimal Ena function. Phosphorylation of Ena by Abl inhibited the binding of Ena to SH3 domains in vitro, suggesting that one effect of Ena phosphorylation may be to modulate its association with other proteins.

PubMed ID
PubMed Central ID
PMC121469 (PMC) (EuropePMC)
DOI
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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Mol. Cell. Biol.
    Title
    Molecular and Cellular Biology
    Publication Year
    1981-
    ISBN/ISSN
    0270-7306
    Data From Reference
    Alleles (6)
    Genes (5)
    Physical Interactions (3)
    Cell Lines (1)
    Natural transposons (1)
    Insertions (1)
    Experimental Tools (2)
    Transgenic Constructs (2)