A novel guanine nucleotide exchange factor MyoGEF is required for cytokinesis.
The cleavage furrow is created by an actomyosin contractile ring that is regulated by small GTPase proteins such as Rac1 and RhoA. Guanine nucleotide exchange factors (GEFs) are positive regulators of the small GTPase proteins and have been implicated as important factors in regulating cytokinesis. However, it is still unclear how GEFs regulate the contractile ring during cytokinesis in mammalian cells. Here we report that a novel GEF, which is termed MyoGEF (myosin-interacting GEF), interacts with non-muscle myosin II and exhibits activity toward RhoA. MyoGEF and non-muscle myosin II colocalize to the cleavage furrow in early anaphase cells. Disruption of MyoGEF expression in U2OS cells by RNA interference (RNAi) results in the formation of multinucleated cells. These results suggest that MyoGEF, RhoA, and non-muscle myosin II act as a functional unit at the cleavage furrow to advance furrow ingression during cytokinesis.
Wu
Di
D
Department of Biochemistry, Kansas State University, Manhattan, Kansas 66506, USA.
Asiedu
Michael
M
Adelstein
Robert S
RS
Wei
Qize
Q
D000818:Animals; D002460:Cell Line; D048749:Cytokinesis; D020662:Guanine Nucleotide Exchange Factors / Q000502:physiology*; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D024462:Myosin Type II / Q000502:physiology; D034741:RNA, Small Interfering / Q000494:pharmacology; D020742:rhoA GTP-Binding Protein / Q000502:physiology
D020662:Guanine Nucleotide Exchange Factors; C527325:PLEKHG6 protein, human; D034741:RNA, Small Interfering; D024462:Myosin Type II; D020742:rhoA GTP-Binding Protein