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Etd1p is a novel protein that links the SIN cascade with cytokinesis
Author(s) -
Daga Rafael R,
Lahoz Aurelia,
Muñoz Manuel J,
Moreno Sergio,
Jimenez Juan
Publication year - 2005
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/sj.emboj.7600705
Subject(s) - cytokinesis , biology , microbiology and biotechnology , mitosis , mitotic exit , septin , schizosaccharomyces , cell division , interphase , aurora b kinase , spindle apparatus , cell , schizosaccharomyces pombe , biochemistry , yeast , saccharomyces cerevisiae
In animal cells, cytokinesis occurs by constriction of an actomyosin ring. In fission yeast cells, ring constriction is triggered by the septum initiation network (SIN), an SPB‐associated GTPase‐regulated kinase cascade that coordinates exit from mitosis with cytokinesis. We have identified a novel protein, Etd1p, required to trigger actomyosin ring constriction in fission yeasts. This protein is localised at the cell tips during interphase. In mitosis, it relocates to the medial cortex region and, coincident with cytokinesis, it assembles into the actomyosin ring by association to Cdc15p. Relocation of Etd1p from the plasma membrane to the medial ring is triggered by SIN signalling and, reciprocally, relocation of the Sid2p–Mob1p kinase complex from the SPB to the division site, a late step in the execution of the SIN, requires Etd1p. These results suggest that Etd1p coordinates the mitotic activation of SIN with the initiation of actomyosin ring constriction. Etd1p peaks during cytokinesis and is degraded by the ubiquitin‐dependent 26S‐proteasome pathway at the end of septation, providing a mechanism to couple inactivation of SIN to completion of cytokinesis.