Shugoshin collaborates with protein phosphatase 2A to protect cohesin (Q24307927)

2

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Kei-ichiro Ishiguro

3

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Shun-ichiro Iemura

4

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Tohru Natsume

5

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Shigehiro A Kawashima

6

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Yoshinori Watanabe

Disseminating the genome: joining, resolving, and separating sister chromatids during mitosis and meiosis

7

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language of work or name

English

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publication date

4 May 2006

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published in

Nature

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volume

441

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page(s)

46-52

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issue

7089

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cites work

1 reference

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Dynamic molecular linkers of the genome: the first decade of SMC proteins

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Kinetochore orientation in mitosis and meiosis.

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Chromosome cohesion and separation: from men and molecules

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The molecular basis of sister-chromatid cohesion

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Shugoshin: guardian spirit at the centromere

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The conserved kinetochore protein shugoshin protects centromeric cohesion during meiosis.

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A genome-wide screen identifies genes required for centromeric cohesion

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Maintenance of cohesin at centromeres after meiosis I in budding yeast requires a kinetochore-associated protein related to MEI-S332.

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A REC8-dependent plant Shugoshin is required for maintenance of centromeric cohesion during meiosis and has no mitotic functions

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Vertebrate shugoshin links sister centromere cohesion and kinetochore microtubule stability in mitosis

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Human Bub1 defines the persistent cohesion site along the mitotic chromosome by affecting Shugoshin localization

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Shugoshin prevents dissociation of cohesin from centromeres during mitosis in vertebrate cells

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The dissociation of cohesin from chromosomes in prophase is regulated by Polo-like kinase

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Dissociation of cohesin from chromosome arms and loss of arm cohesion during early mitosis depends on phosphorylation of SA2.

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Cohesin release is required for sister chromatid resolution, but not for condensin-mediated compaction, at the onset of mitosis

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Phosphorylation of the cohesin subunit Scc1 by Polo/Cdc5 kinase regulates sister chromatid separation in yeast

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Preferential cleavage of chromatin-bound cohesin after targeted phosphorylation by Polo-like kinase

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Role of Polo-like kinase CDC5 in programming meiosis I chromosome segregation

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Polo-like kinase Cdc5 promotes chiasmata formation and cosegregation of sister centromeres at meiosis I.

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Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling

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Human Bub1 protects centromeric sister-chromatid cohesion through Shugoshin during mitosis

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Okadaic acid inhibits a protein phosphatase activity involved in formation of the mitotic spindle of GH4 rat pituitary cells

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Distinct, essential roles of type 1 and 2A protein phosphatases in the control of the fission yeast cell division cycle.

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Okadaic acid, an inhibitor of protein phosphatase 1 and 2A, induces premature separation of sister chromatids during meiosis I and aneuploidy in mouse oocytes in vitro

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The core centromere and Sgo1 establish a 50-kb cohesin-protected domain around centromeres during meiosis I

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POLO kinase regulates the Drosophila centromere cohesion protein MEI-S332.

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PP2A: the expected tumor suppressor

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Identification of a consensus motif for Plk (Polo-like kinase) phosphorylation reveals Myt1 as a Plk1 substrate.

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The small molecule Hesperadin reveals a role for Aurora B in correcting kinetochore-microtubule attachment and in maintaining the spindle assembly checkpoint

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Molecular biology. SMC complexes--wrapped up in controversy

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inferred from DOI database lookup

7 January 2021

based on heuristic

A direct nanoflow liquid chromatography-tandem mass spectrometry system for interaction proteomics

1 reference

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inferred from DOI database lookup

7 January 2021

based on heuristic

The protein phosphatase 2A B'-regulatory subunit par1p is implicated in regulation of the S. pombe septation initiation network

1 reference

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inferred from DOI database lookup

7 January 2021

based on heuristic

Inhibition of mitosis by okadaic acid: possible involvement of a protein phosphatase 2A in the transition from metaphase to anaphase

1 reference

4 November 2023

https://opencitations.net/index/coci/api/v1/references/10.1038/NATURE04663

Identifiers

DOI

10.1038/NATURE04663

1 reference

Consolidated OpenCitations Corpus – April 2017

Dimensions Publication ID

449998

1034816995

0 references

Fatcat ID

release_3nkxxpkvrfeytbwgh2wxcknnqu

0 references

449998

1 reference

Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

1 reference