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Título

Hob3p, the fission yeast ortholog of human BIN3, localizes Cdc42p to the division site and regulates cytokinesis

AutorColl, Pedro M.; Rincón Padilla, Sergio A.; Pérez González, Pilar; Izquierdo, Raul
Palabras claveAmphiphysin
Cdc42
Cytokinesis
Fission yeast
GEF
GTPases
Fecha de publicaciónabr-2007
EditorNature Publishing Group
CitaciónEMBO J. 2007 April 4; 26(7): 1865–1877
ResumenCdc42 GTPase is required for polarization in eukaryotic cells, but its spatial regulation is poorly understood. In Schizosaccharomyces pombe, Cdc42p is activated by Scd1p and Gef1p, two guanine-nucleotide exchange factors. Two-hybrid screening identified Hob3p as a Gef1p binding partner. Hob3p is a BAR domain-containing protein ortholog of human Bin3. Hob3p also interacts directly with Cdc42p independently of Gef1p. Hob3p, Cdc42p and Gef1p form a complex, and Hob3p facilitates Gef1p–Cdc42p interaction and activation. Hob3p forms a ring in the division area, similar to that of Gef1p. This localization requires actin polymerization and Cdc15p but is independent of the septation initiation network. Hob3p is required for the concentration of Cdc42p to the division area. The actomyosin ring contraction is slower in hob3Δ than in wild-type cells, and this contributes to its cytokinesis defect. Moreover, this report extends previous evidence that human Bin3 suppresses the cytokinesis phenotype of hob3Δ cells, showing that Bin3 can partially recover the GTP-Cdc42p level and its localization. These results suggest that Hob3p is required to recruit and activate Cdc42p at the cell division site and that this function might be conserved in other eukaryotes.
DescripciónFinal full-text version of the paper available at: http://www.nature.com/emboj/journal/v26/n7/index.html
URIhttp://hdl.handle.net/10261/5173
DOI10.1038/sj.emboj.7601641
ISSN1460-2075
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