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Molecular and Cellular Biology, October 2002, p. 6854-6865, Vol. 22, No. 19
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.19.6854-6865.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Phyllopod Acts as an Adaptor Protein To Link the Sina Ubiquitin Ligase to the Substrate Protein Tramtrack

Songhui Li,{dagger} Chunyan Xu,{ddagger} and Richard W. Carthew*

Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208

Received 31 January 2002/ Returned for modification 26 March 2002/ Accepted 19 June 2002

The RING domain protein Sina, together with Phyllopod and the F-box protein Ebi, forms a Ras-regulated E3 ubiquitin ligase complex that activates photoreceptor cell differentiation in the eye of Drosophila melanogaster. The expression of Phyllopod is induced upon Ras activation, allowing the complex to degrade the transcription repressor Tramtrack and removing its block of neuronal development in photoreceptor precursors. We show that Phyllopod functions as an adaptor in the complex, physically linking Sina with Tramtrack via separate binding domains. One 19-amino-acid domain in Phyllopod interacts with a region of Sina's SBD domain. Another domain in Phyllopod interacts with a C-terminal helix in the POZ domain of Tramtrack. This interaction is specific to the Tramtrack POZ domain and not to other POZ domain proteins present in photoreceptor precursors. Degradation of Tramtrack is dependent upon association of Sina with its cognate binding site in Phyllopod. These results illustrate how Ras signaling can modulate an E3 ligase activity not by the phosphorylation of substrate proteins but by regulating the expression of specific E3 adaptors.

* Corresponding author. Mailing address: Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, IL 60208. Phone: (847) 467-4891. Fax: (847) 467-1380. E-mail: r-carthew{at}northwestern.edu.

{dagger} Present address: Department of Pathology, University of Pittsburgh School of Medicine, Pittsburgh, PA 15261.

{ddagger} Present address: Center for Computational Biology and Bioinformatics, University of Pittsburgh School of Medicine, Pittsburgh, PA 15213.

Molecular and Cellular Biology, October 2002, p. 6854-6865, Vol. 22, No. 19
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.19.6854-6865.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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