期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 102, 期 46, 页码 16584-16589出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0508306102
关键词
cell division; G protein; GoLoco; GPR; guanine nucleotide exchange
资金
- NIGMS NIH HHS [R37 GM034497, R01 GM034497, GM34497] Funding Source: Medline
Resistance to inhibitors of cholinesterase (Ric) 8A is a guanine nucleotide exchange factor that activates certain G protein alpha-subunits. Genetic studies in Caenorhabditis elegans and Drosophila melanogaster have placed RIC-8 in a previously uncharacterized G protein signaling pathway that regulates centrosome movements during cell division. Components of this pathway include G protein subunits of the G alpha i class, GPR or GoLoco domain-containing proteins, RGS (regulator of G protein signaling) proteins, and accessory factors. These proteins interact to regulate microtubule pulling forces during mitotic movement of chromosomes. It is unclear how the GTP-binding and hydrolysis cycle of Gai functions in the context of this pathway. In mammals, the GoLoco domain-containing protein LGN (GPSM2), the LGN- and microtubule-binding nuclear mitotic apparatus protein (NuMA), and Gai regulate a similar process. We find that mammalian Ric-8A dissociates G alpha i-GDP/LGN/ NuMA complexes catalytically, releasing activated G alpha i-GTP in vitro. Ric-8A-stimulated activation of G alpha i caused concomitant liberation of NuMA from LGN. We conclude that Ric-8A efficiently utilizes GoLoco/G alpha i-GDP complexes as substrates in vitro and suggest that Ric-8A-stimulated release of Gai-GTP and/or NuMA regulates the microtubule pulling forces on centrosomes during cell division.
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