Dialogue between centrosomal entrance and exit scaffold pathways regulates mitotic commitment.

2.50
Hdl Handle:
http://hdl.handle.net/10541/620556
Title:
Dialogue between centrosomal entrance and exit scaffold pathways regulates mitotic commitment.
Authors:
Chan, Kuan Yoow; Alonso-Nuñez, Marisa; Grallert, Agnes; Tanaka, Kayoko; Connolly, Yvonne; Smith, Duncan L; Hagan, Iain M
Abstract:
The fission yeast scaffold molecule Sid4 anchors the septum initiation network to the spindle pole body (SPB, centrosome equivalent) to control mitotic exit events. A second SPB-associated scaffold, Cut12, promotes SPB-associated Cdk1-cyclin B to drive mitotic commitment. Signals emanating from each scaffold have been assumed to operate independently to promote two distinct outcomes. We now find that signals from Sid4 contribute to the Cut12 mitotic commitment switch. Specifically, phosphorylation of Sid4 by NIMA(Fin1) reduces Sid4 affinity for its SPB anchor, Ppc89, while also enhancing Sid4's affinity for casein kinase 1δ (CK1δ). The resulting phosphorylation of Sid4 by the newly docked CK1δ recruits Chk2(Cds1) to Sid4. Chk2(Cds1) then expels the Cdk1-cyclin B antagonistic phosphatase Flp1/Clp1 from the SPB. Flp1/Clp1 departure can then support mitotic commitment when Cdk1-cyclin B activation at the SPB is compromised by reduction of Cut12 function. Such integration of signals emanating from neighboring scaffolds shows how centrosomes/SPBs can integrate inputs from multiple pathways to control cell fate.
Affiliation:
Cell Division Group, Cancer Research UK Manchester Institute, University of Manchester, Manchester, England, UK
Citation:
Dialogue between centrosomal entrance and exit scaffold pathways regulates mitotic commitment. 2017, 216 (9):2795-2812 J. Cell Biol.
Journal:
The Journal of Cell Biology
Issue Date:
4-Sep-2017
URI:
http://hdl.handle.net/10541/620556
DOI:
10.1083/jcb.201702172
PubMed ID:
28774892
Type:
Article
Language:
en
ISSN:
1540-8140
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorChan, Kuan Yoowen
dc.contributor.authorAlonso-Nuñez, Marisaen
dc.contributor.authorGrallert, Agnesen
dc.contributor.authorTanaka, Kayokoen
dc.contributor.authorConnolly, Yvonneen
dc.contributor.authorSmith, Duncan Len
dc.contributor.authorHagan, Iain Men
dc.date.accessioned2017-09-08T15:03:25Z-
dc.date.available2017-09-08T15:03:25Z-
dc.date.issued2017-09-04-
dc.identifier.citationDialogue between centrosomal entrance and exit scaffold pathways regulates mitotic commitment. 2017, 216 (9):2795-2812 J. Cell Biol.en
dc.identifier.issn1540-8140-
dc.identifier.pmid28774892-
dc.identifier.doi10.1083/jcb.201702172-
dc.identifier.urihttp://hdl.handle.net/10541/620556-
dc.description.abstractThe fission yeast scaffold molecule Sid4 anchors the septum initiation network to the spindle pole body (SPB, centrosome equivalent) to control mitotic exit events. A second SPB-associated scaffold, Cut12, promotes SPB-associated Cdk1-cyclin B to drive mitotic commitment. Signals emanating from each scaffold have been assumed to operate independently to promote two distinct outcomes. We now find that signals from Sid4 contribute to the Cut12 mitotic commitment switch. Specifically, phosphorylation of Sid4 by NIMA(Fin1) reduces Sid4 affinity for its SPB anchor, Ppc89, while also enhancing Sid4's affinity for casein kinase 1δ (CK1δ). The resulting phosphorylation of Sid4 by the newly docked CK1δ recruits Chk2(Cds1) to Sid4. Chk2(Cds1) then expels the Cdk1-cyclin B antagonistic phosphatase Flp1/Clp1 from the SPB. Flp1/Clp1 departure can then support mitotic commitment when Cdk1-cyclin B activation at the SPB is compromised by reduction of Cut12 function. Such integration of signals emanating from neighboring scaffolds shows how centrosomes/SPBs can integrate inputs from multiple pathways to control cell fate.en
dc.language.isoenen
dc.rightsArchived with thanks to The Journal of cell biologyen
dc.titleDialogue between centrosomal entrance and exit scaffold pathways regulates mitotic commitment.en
dc.typeArticleen
dc.contributor.departmentCell Division Group, Cancer Research UK Manchester Institute, University of Manchester, Manchester, England, UKen
dc.identifier.journalThe Journal of Cell Biologyen

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