High impact information on Sra-1

• WAVE function is regulated through a protein complex containing Sra1, Kette and Abi [1].
• Finally, CYFIP acts as a dRac1 effector that antagonizes FMR1 function, providing a bridge between signal-dependent cytoskeleton remodeling and translation [2].
• Outgrowing photoreceptor neurons express high levels of Sra-1 also in growth cones [3].
• During late embryonic and larval development, the Sra-1 protein is found in the neuropile [3].
• Hyperactivation of calcineurin signaling in the germline cells resulted in a meiotic-arrest phenotype, which can also be suppressed by overexpression of Sra [4].

Biological context of Sra-1

• Similar mutant phenotypes were induced after expression of membrane-bound Sra-1 that lacks the Kette-binding domain, suggesting that sra-1 function is mediated through kette [3].
• All these results support the hypothesis that Sra regulates female meiosis by controlling calcineurin activity in the germline [4].
• Sra is physically associated with the catalytic subunit of calcineurin, and its overexpression suppresses the phenotypes caused by constitutively activated calcineurin, such as rough eye or loss of wing veins [4].

Anatomical context of Sra-1

• Here we show that the Drosophila proteins SCAR, CYFIP and Kette, orthologs of WAVE/SCAR complex components, all show strong accumulation in axons of the central nervous system and indeed form a complex in vivo [5].

Other interactions of Sra-1

• We also show that RNAi of three proteins (kette, Abi, and Sra-1) known to copurify with and inhibit SCAR in vitro leads to SCAR degradation, revealing a novel function of this protein complex in SCAR stability [6].

References