Proteins keep Cdc55 in its place
نویسنده
چکیده
Proteins keep Cdc55 in its place R ossio and Yoshida reveal how cells control the location of the mitosis-regulating protein Cdc55. Cdc55 is a key component of the protein phosphatase 2A (PP2A) complex, which helps determine when cells begin and end mitosis. Two other proteins, Zds1 and Zds2, keep the complex under control. They switch on PP2A to nudge the cell into mitosis and switch it off to spur the cell to exit mitosis. Rossio and Yoshida wanted to investigate how this regulation occurs. The researchers tracked the locations of Zds1, Zds2, and Cdc55 in budding yeast cells. Zds1 and Zds2 stayed exclusively in the cytoplasm, whereas Cdc55 could also enter the nucleus. To determine whether Cdc55’s location altered its effect on mitosis, Rossio and Yoshida created mutant versions of the protein that remained either in the nucleus or the cytoplasm. Cells that harbored the cytoplasm-only Cdc55 form started mitosis normally, but yeast that made the exclusively nuclear version procrastinated, delaying the beginning of mitosis. In the absence of Zds1 and Zds2, Cdc55 built up in the nucleus, where it prolonged mitosis by hindering the release of Cdc14, which normally helps push the cell into G1. The researchers think that Zds1 and Zds2 play a dual role. They trap Cdc55 in the cytoplasm, where it can prompt the cell to initiate mitosis. And because the proteins prevent Cdc55 from moving on to the nucleus, they allow the cell to exit mitosis. Rossio, V., and S. Yoshida. 2011. J. Cell Biol. doi:10.1083/jcb.201101134.
منابع مشابه
The Zds proteins control entry into mitosis and target protein phosphatase 2A to the Cdc25 phosphatase
The Wee1 kinase restrains entry into mitosis by phosphorylating and inhibiting cyclin-dependent kinase 1 (Cdk1). The Cdc25 phosphatase promotes entry into mitosis by removing Cdk1 inhibitory phosphorylation. Experiments in diverse systems have established that Wee1 and Cdc25 are regulated by protein phosphatase 2A (PP2A), but a full understanding of the function and regulation of PP2A in entry ...
متن کاملSpatial regulation of Cdc55–PP2A by Zds1/Zds2 controls mitotic entry and mitotic exit in budding yeast
Budding yeast CDC55 encodes a regulatory B subunit of the PP2A (protein phosphatase 2A), which plays important roles in mitotic entry and mitotic exit. The spatial and temporal regulation of PP2A is poorly understood, although recent studies demonstrated that the conserved proteins Zds1 and Zds2 stoichiometrically bind to Cdc55-PP2A and regulate it in a complex manner. Zds1/Zds2 promote Cdc55-P...
متن کاملA - Cdc 55 prevents APC - Cdc 20 activation during the spindle assembly checkpoint
Cdc55, a regulatory B-subunit of PP2A complex, is essential for the Spindle Assembly Checkpoint (SAC) in budding yeast, but regulation and molecular targets of PP2A-Cdc55 have not been clearly defined or controversial. Here we show that an important target of Cdc55 in the SAC is Anaphase Promoting Complex (APC) coupled with Cdc20 and that APC-Cdc20 is kept inactive by dephosphorylation by nucle...
متن کاملA - Cdc 55 prevents APC - Cdc 20 activation during the spindle assembly checkpoint ( SAC )
Cdc55, a regulatory B-subunit of PP2A complex, is essential for the Spindle Assembly Checkpoint (SAC) in budding yeast, but regulation and molecular targets of PP2A-Cdc55 have not been clearly defined or controversial. Here we show that an important target of Cdc55 in the SAC is Anaphase Promoting Complex (APC) coupled with Cdc20 and that APC-Cdc20 is kept inactive by dephosphorylation by nucle...
متن کاملNuclear PP2A-Cdc55 prevents APC-Cdc20 activation during the spindle assembly checkpoint.
Cdc55, a regulatory B-subunit of protein phosphatase 2A (PP2A) complex, is essential for the spindle assembly checkpoint (SAC) in budding yeast, but the regulation and molecular targets of PP2A-Cdc55 have not been clearly defined or are controversial. Here, we show that an important target of Cdc55 in the SAC is the anaphase-promoting complex (APC) coupled with Cdc20 and that APC-Cdc20 is kept ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
دوره 193 شماره
صفحات -
تاریخ انتشار 2011