The GoLoco motif: heralding a new tango between G protein signaling and cell division.
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.
Kimple
Randall J
RJ
Department of Pharmacology, Lineberger Comprehensive Cancer Center, UNC Neuroscience Center, The University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-7365, USA.
Willard
Francis S
FS
Siderovski
David P
DP
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D002455:Cell Division; D020962:Heterotrimeric GTP-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009474:Neurons / Q000166:cytology*; D015398:Signal Transduction
D020962:Heterotrimeric GTP-Binding Proteins