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PNAS 103 (17): 6524-6529

Copyright © 2006 by the National Academy of Sciences.

BIOLOGICAL SCIENCES / CELL BIOLOGY

Dual roles for the trimeric G protein Go in asymmetric cell division in Drosophila

Vladimir L. Katanaev*, and Andrew Tomlinson{dagger}

Department of Genetics and Development, College of Physicians and Surgeons, Columbia University, 701 West 168th Street, Suite 1120, New York, NY 10032

Communicated by Richard Axel, Columbia University, New York, NY, March 7, 2006

Received for publication July 15, 2005.

Abstract: During asymmetric division, a cell polarizes and differentially distributes components to its opposite ends. The subsequent division differentially segregates the two component pools to the daughters, which thereby inherit different developmental directives. In Drosophila sensory organ precursor cells, the localization of Numb protein to the cell's anterior cortex is a key patterning event and is achieved by the combined action of many proteins, including Pins, which itself is localized anteriorly. Here, a role is described for the trimeric G protein Go in the anterior localization of Numb and daughter cell fate specification. Go is shown to interact with Pins. In addition to a role in recruiting Numb to an asymmetric location in the cell's cortex, Go transduces a signal from the Frizzled receptor that directs the position in which the complex forms. Thus, Go likely integrates the signaling that directs the formation of the complex with the signaling that directs where the complex forms.

Key Words: Frizzled • cell polarization • signal transduction

Freely available online through the PNAS open access option.

*Present address: Department of Biology, University of Konstanz, 78467 Konstanz, Germany.

Author contributions: V.L.K. and A.T. designed research; V.L.K. performed research; V.L.K. contributed new reagents/analytic tools; V.L.K. and A.T. analyzed data; and V.L.K. and A.T. wrote the paper.

Conflict of interest statement: No conflicts declared.

{dagger}To whom correspondence should be addressed. E-mail: at41{at}columbia.edu

© 2006 by The National Academy of Sciences of the USA

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