The Drosophila primo locus encodes two low-molecular-weight tyrosine phosphatases
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Updated: Oct 17, 2026

Medium-scale Preparation of Drosophila Embryo Extracts for Proteomic Experiments
Published on: May 30, 2017
D T Miller1, R Read, J Rusconi
1Department of Molecular Biology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO, USA.
Abstract:
The fine modulation of tyrosine phosphorylation by protein tyrosine phosphatases and protein tyrosine kinases is a key regulatory mechanism for many cell signaling pathways active during development. In a screen for genes with interesting expression patterns in the developing Drosophila pupal retina, we identified a novel pair of protein tyrosine phosphatases that exhibit an expression pattern suggesting a role in multiple steps of Drosophila neurogenesis. Together, these phosphatases define the primo locus. Their sequence is approx. 50% identical to each other and to low-molecular-weight protein tyrosine phosphatases (LMW-PTPs) identified in other species. Little is understood of the biological role of LMW-PTPs, and the powerful tools available in Drosophila should provide important insight into their role in signaling and development.
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