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The GoLoco Motif: Heralding a New Tango Between G Protein Signaling and Cell Division

Department of Pharmacology Lineberger Comprehensive Cancer Center Unc Neuroscience Center The University of North Carolina at Chapel Hill Chapel Hill NC 27599-7365 USA

Correspondence: DPS. E-mail dsiderov{at}med.unc.edu; fax 919-966-5640.

Heterotrimeric G proteins regulate signaling pathways downstream of plasma membrane-bound receptors. Several mechanisms have been discovered that promote the separate effector functions of the G and the Gß subunits. Recent efforts have identified GoLoco motif-containing proteins as G-associated proteins that can regulate the reassociation of G to Gß, and that might effect signal transduction on their own. In what physiological processes are these proteins involved?

The G and Gß components of heterotrimeric G proteins, typically associated with cell-surface receptor signaling, also partake in the macromolecular interactions that underlie cell polarity and cell division. Proteins with G-binding GoLoco motifs, such as Drosophila melanogaster Pins (for Partner of Inscuteable) and its mammalian counterpart LGN, participate in multi-protein complexes that maintain cellular asymmetry and orderly segregation of chromosomal content and daughter cell bodies. The GoLoco motif was recently identified as a selective G-binding partner: the GoLoco–G interaction can displace Gß and inhibit guanine nucleotide release from the bound G subunit. Recent x-ray crystallographic studies suggest ways in which GoLoco-motif peptides may modulate heterotrimeric G protein signaling. Such peptides could be exploited to help dissect the signals that underpin cell polarity and cell division processes.

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