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Vol. 14, No. 2, pp. 177-186, January 15, 2000
homolog Spitz
Molecular Neurobiology Laboratory, The Salk Institute for Biological
Studies, La Jolla, California 92037 USA
Activation of the Drosophila epidermal growth factor
receptor (DER) by the transmembrane ligand, Spitz (Spi), requires two additional transmembrane proteins, Rhomboid and Star. Genetic evidence
suggests that Rhomboid and Star facilitate DER signaling by processing
membrane-bound Spi (mSpi) to an active, soluble form. To test this
model, we use an assay based on Xenopus animal cap explants in
which Spi activation of DER is Rhomboid and Star dependent. We show
that Spi is on the cell surface but is kept in an inactive state by its
cytoplasmic and transmembrane domains; Rhomboid and Star relieve this
inhibition, allowing Spi to signal. We show further that Spi is likely
to be cleaved within its transmembrane domain. However, a mutant form
of mSpi that is not cleaved still signals to DER in a Rhomboid and
Star-dependent manner. These results suggest strongly that Rhomboid and
Star act primarily to present an active form of Spi to DER, leading
secondarily to the processing of Spi into a secreted form.
[Key Words: spitz; rhomboid; Star; EGFR; Drosophila; Xenopus animal caps]
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