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PMID:17981136

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Citation

Joo, E, Surka, MC and Trimble, WS (2007) Mammalian SEPT2 is required for scaffolding nonmuscle myosin II and its kinases. Dev. Cell 13:677-90

Abstract

Mammalian septin SEPT2 belongs to a conserved family of filamentous GTPases that are associated with actin stress fibers in interphase cells and the contractile ring in dividing cells. Although SEPT2 is essential for cytokinesis, its role in this process remains undefined. Here, we report that SEPT2 directly binds nonmuscle myosin II (myosin II), and this association is important for fully activating myosin II in interphase and dividing cells. Inhibition of the SEPT2-myosin II interaction in interphase cells results in loss of stress fibers, while in dividing cells this causes instability of the ingressed cleavage furrow and dissociation of the myosin II from the Rho-activated myosin kinases ROCK and citron kinase. We propose that SEPT2-containing filaments provide a molecular platform for myosin II and its kinases to ensure the full activation of myosin II that is necessary for the final stages of cytokinesis.

Links

PubMed Online version:10.1016/j.devcel.2007.09.001

Keywords

Animals; CHO Cells; Cricetinae; Cricetulus; Cytokinesis; GTP Phosphohydrolases/physiology; Intracellular Signaling Peptides and Proteins/metabolism; Myosin Type II/metabolism; Protein Binding; Protein Folding; Protein-Serine-Threonine Kinases/metabolism; rho-Associated Kinases/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

CRIGR:G3H4V1

Colocalizes with

GO:0016460: myosin II complex

ECO:0000314:

C

Cricetulus griseus; Septin-2 (SEPT2)

In Figure 1A, immunostaining of myosin-II and SEPT2 in the cells of Chinese hamsters shows that they colocalize.

complete
CACAO 12952

Notes

See also

References

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