ArticleThe Biochemical journal2002
Expression in mammalian cell cultures reveals interdependent, but distinct, functions for Star and Rhomboid proteins in the processing of the Drosophila transforming-growth-factor-alpha homologue Spitz.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed, 19 citations in OpenAlex.
- The role of protease activity in ErbB biology.Experimental cell research · 2009Review
- Breast cancer molecular signatures as determined by SAGE: correlation with lymph node status.Molecular cancer research : MCR · 2007Article
- A family of Rhomboid intramembrane proteases activates all Drosophila membrane-tethered EGF ligands.The EMBO journal · 2002Article
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3 authors at 1 institution in 1 country.
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Abstract
We report here distinct interdependent functions for two proteins, Star and Rhomboid, that are key determinants of the epidermal-growth-factor (EGF)-receptor signalling pathway in Drosophila. When we expressed the Drosophila EGF-receptor ligand Spitz in mammalian cells, the protein failed to traffic to the plasma membrane, as assessed by either cell-surface protein biotinylation or immunocytochemical staining. However, when we co-expressed Star with Spitz, trafficking of Spitz to the cell surface could be demonstrated. Only when we co-expressed Spitz, Star and Rhomboid could the release of soluble Spitz protein into the medium be shown. Taken together, our results indicate that Star is required for the intracellular trafficking of Spitz, and that Rhomboid is essential for the release of soluble Spitz protein from cells.
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