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Gene Review:

Dab - Disabled

Drosophila melanogaster

Synonyms: CG9695, Dmel\CG9695, Protein disabled, cDNA C, dab

Howell, B.W. et al., Yun, M. et al., Gertler, F.B. et al., Le, N. et al., Winder, S.J.

Winder,

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High impact information on Dab

Embryos that are homozygous mutant for both abl and dab fail to develop any axon bundles in the CNS, although the peripheral nervous system and the larval cuticle appear normal [1].
Here, we identify a mouse homolog of the Drosophila Disabled (Dab) protein, mDab1, and show it is an adaptor molecule functioning in neural development [2].
The properties of mDab1 and genetic analysis of Dab in Drosophila suggest that these molecules function in key signal transduction pathways involved in the formation of neural networks [2].
We show that the phosphotyrosine-binding (PTB) domain-containing protein Disabled (DAB) binds to the DRK SH3 domains [3].
These findings suggest that simultaneous interaction of the rigid DH domain with the NPXY sequence and PtdIns-4,5-P2 plays a role in the attachment of Dab proteins to the APP/lipoprotein receptors and phosphoinositide-rich membranes [4].

Other interactions of Dab

Two prominent genes that arose from these screens were enabled (Ena) and disabled (Dab) [5].

References

Drosophila abl tyrosine kinase in embryonic CNS axons: a role in axonogenesis is revealed through dosage-sensitive interactions with disabled. Gertler, F.B., Bennett, R.L., Clark, M.J., Hoffmann, F.M. Cell (1989) [Pubmed]
Mouse disabled (mDab1): a Src binding protein implicated in neuronal development. Howell, B.W., Gertler, F.B., Cooper, J.A. EMBO J. (1997) [Pubmed]
Disabled is a putative adaptor protein that functions during signaling by the sevenless receptor tyrosine kinase. Le, N., Simon, M.A. Mol. Cell. Biol. (1998) [Pubmed]
Crystal structures of the Dab homology domains of mouse disabled 1 and 2. Yun, M., Keshvara, L., Park, C.G., Zhang, Y.M., Dickerson, J.B., Zheng, J., Rock, C.O., Curran, T., Park, H.W. J. Biol. Chem. (2003) [Pubmed]
Filopodia formation and Disabled degradation downstream of Reelin. Winder, S.J. Biochem. J. (2004) [Pubmed]

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