The GoLoco motif: heralding a new tango between G protein signaling and cell division |
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Authors: | Kimple Randall J Willard Francis S Siderovski David P |
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Affiliation: | Department of Pharmacology, Lineberger Comprehensive Cancer Center, UNC Neuroscience Center, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7365, USA. |
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Abstract: | The Galpha and Gbetagamma 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 Galpha-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 Galpha-binding partner: the GoLoco-Galpha interaction can displace Gbetagamma and inhibit guanine nucleotide release from the bound Galpha 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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