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Updated: Sep 25, 2026

Detection of In Situ Protein-protein Complexes at the Drosophila Larval Neuromuscular Junction Using Proximity Ligation Assay
Published on: January 20, 2015
L63, the Drosophila PFTAIRE, interacts with two novel proteins unrelated to cyclins
Anne Rascle1, R Steven Stowers, Dan Garza
1Departments of Biochemistry and Developmental Biology, Stanford University School of Medicine, Stanford, CA 94305, USA. anne.rascle@dnax.org
Abstract:
L63 encodes a CDK-like protein homologous to the mammalian PFTAIRE. We showed previously that L63 provides a CDK-related function critical to development (Dev. Biol. 221 (2000) 23). We present here the first biochemical characterization of L63 kinase. In addition, we describe two novel Drosophila proteins, PIF-1 and PIF-2 (for PFTAIRE Interacting Factor-1 and -2), identified in a two-hybrid screen for their ability to interact with the amino-terminal region of L63. The full-length PIF-1 cDNA shows an unusual dicistronic organization. PIF-1A and PIF-1B (the L63 interactor) predicted proteins are expressed in vivo, and show a distinct expression profile during development. Interaction between L63 and PIF-1B was confirmed in vitro and in vivo. The role of this interaction remains to be demonstrated, but our data suggest that PIF-1B might serve as a regulator of L63.
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