期刊
ANNUAL REVIEW OF BIOCHEMISTRY
卷 73, 期 -, 页码 925-951出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev.biochem.73.011303.073756
关键词
asymmetric cell division; guanine nucleotide dissociation inhibitors; heterotrimeric G proteins; RGS proteins
资金
- NIGMS NIH HHS [GM062338, GM065533] Funding Source: Medline
- NIMH NIH HHS [F30 MH064319] Funding Source: Medline
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [P01GM065533, R01GM062338] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF MENTAL HEALTH [F30MH064319] Funding Source: NIH RePORTER
The GoLoco motif is a 19-amino-acid sequence with guanine nucleotide dissociation inhibitor activity against G-alpha subunits of the adenylyl-cyclase-inhibitory subclass. The GoLoco motif is present as an independent element within multidomain signaling regulators, such as Loco, RGS12, RGS14, and Rap1GAP, as well as in tandem arrays in proteins, such as AGS3, G18, LGN, Pcp-2/L7, and Partner of Inscuteable (Pins/Rapsynoid). Here we discuss the biochemical mechanisms of GoLoco motif action on G-alpha subunits in light of the recent crystal structure of G-alpha-i1 bound to the RGS14 GoLoco motif. Currently, there is sparse evidence for GoLoco motif regulation of canonical G-protein-coupled receptor signaling. Rather, studies of asymmetric cell division in Drosophila and Caenorhabditis elegans, as well as mammalian mitosis, implicate GoLoco proteins, such as Pins, GPR-1/GPR-2, LGN, and RGS14, in mitotic spindle organization and force generation. We discuss potential mechanisms by which GoLoco/Galpha complexes might modulate spindle dynamics.
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