AIP regulates stability of Aurora-A at early mitotic phase coordinately with GSK-3β

Fumoto, Katsumi; Lee, Ping Chin; Saya, Hideyuki; Kikuchi, Akira

doi:10.1038/onc.2008.92

Cited by 17 publications

(14 citation statements)

References 31 publications

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“…For example, GSK-3 is able to phosphorylate the Aurora A interacting protein, AIP, acting to limit the activity of centrosomal Aurora A kinase, while recent work has also identified the γ-tubulin ring complex protein GCP5 as a substrate for GSK-3; inhibition of GSK-3 leads to an accumulation of γ-TuRC at the centrosome, and increased MT nucleation. 41,42 Together these data reveal GSK-3 as a key mediator of MT growth during mitosis, though the intricacies of GSK-3 regulation upon spindle organization have yet to be determined.…”

Section: Pi3-k/akt/gsk-3 and Cell Migration And Polaritymentioning

confidence: 92%

PI3-K and GSK-3: Akt-ing together with microtubules

Buttrick¹,

Wakefield²

2008

Cell Cycle

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Section: Pi3-k/akt/gsk-3 and Cell Migration And Polaritymentioning

confidence: 92%

PI3-K and GSK-3: Akt-ing together with microtubules

Buttrick¹,

Wakefield²

2008

Cell Cycle

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“…Indeed, this phosphorylation of Aurora-A at Serine 349 was found to be indispensable for meiosis Glycogen synthase kinase 3 in bovine oocyte progression in Xenopus oocytes (Pascreau et al 2008). In human HeLa cells, it was recently shown that GSK3B finely regulated synthesis and activity of AURKA through binding and phosphorylation of Aurora-A-interacting protein (AIP) during mitosis (Fumoto et al 2008). At the same time, GSK3B, AIP and AURKA were co-localised at the spindle poles, and when AIP was depleted, AURKA remained permanently active and caused a pro-metaphase arrest (Fumoto et al 2008).…”

Section: Gsk3b Expression In Bovine Oocytes and Surrounding Folliculamentioning

confidence: 99%

“…In human HeLa cells, it was recently shown that GSK3B finely regulated synthesis and activity of AURKA through binding and phosphorylation of Aurora-A-interacting protein (AIP) during mitosis (Fumoto et al 2008). At the same time, GSK3B, AIP and AURKA were co-localised at the spindle poles, and when AIP was depleted, AURKA remained permanently active and caused a pro-metaphase arrest (Fumoto et al 2008). We detected active phospho-Thr AURKA in cytoplasm of bovine immature oocytes and at the contractile ring of midbody in mature MII-arrested oocytes (Uzbekova et al 2008).…”

Section: Gsk3b Expression In Bovine Oocytes and Surrounding Folliculamentioning

confidence: 99%

Glycogen synthase kinase 3B in bovine oocytes and granulosa cells: possible involvement in meiosis during in vitro maturation

Uzbekova¹,

Salhab²,

Perreau³

et al. 2009

Reproduction

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Glycogen synthase kinase 3 (GSK3) regulates cellular metabolism and cell cycle via different signalling pathways. In response to insulin and growth factors GSK3 is serine-phosphorylated and inactivated. We analysed GSK3B expression and activation in bovine cumulus cells (CC) and oocytes at different meiotic stages in vitro in parallel with MAP kinases ERK (MAPK3/MAPK1) and p38 (MAPK14). GSK3B localised to cytoplasm in granulosa cells and in oocytes throughout folliculogenesis. In mature metaphase-II (MII) oocytes, GSK3B was concentrated to the region of midzone between the oocyte and the first polar body, as well as active phospho-Thr Aurora A kinase (AURKA). During in vitro maturation (IVM), in oocytes, phospho-Ser 9 -GSK3B level increased as well as phospho-MAPK3/MAPK1, while phospho-MAPK14 decreased. In CC, phospho-MAPK14 increased upon germinal vesicle breakdown (GVBD)/metaphase-I (MI) and then decreased during transition to MII. Administration of inhibitors of GSK3 activity (lithium chloride or 2 0 Z,3 0 E -6-bromoindirubin-3 0 -oxime) rapidly increased phospho-Ser 9 -GSK3B, and led to transient decrease of phospho-MAPK3/MAPK1 and to durable enhancing of phospho-MAPK14 in granulosa primary cell culture. GSK3 inhibitors during IVM diminished cumulus expansion and delayed meiotic progression. In cumulus, phospho-MAPK14 level was significantly higher in the presence of inhibitors, comparing with control, through the time of MI/MII transition. In oocytes, phospho-GSK3B was increased and phospho-MAPK3/MAPK1 was decreased before GVBD and oocytes were mainly arrested at MI. Therefore, GSK3B might regulate oocyte meiosis, notably MI/MII transition being the part of MAPK3/1 and MAPK14 pathways in oocytes and CC. GSK3B might be also involved in the local activation of AURKA that controls this transition.

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“…An alternative pathway for Aurora A degradation involves phosphorylation of AIP1 by GSK3beta [19]. AIP1 localises at the centrosome where it binds and downregulates Aurora A early in mitosis [20]. …”

Section: Introductionmentioning

confidence: 99%

Making the Auroras glow: regulation of Aurora A and B kinase function by interacting proteins

Carmena

Ruchaud

Earnshaw

2009

Current Opinion in Cell Biology

320

314

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The conserved Aurora family of protein kinases have emerged as crucial regulators of mitosis and cytokinesis. Despite their high degree of homology, Aurora A and B have very distinctive localisations and functions: Aurora A associates with the spindle poles to regulate entry into mitosis, centrosome maturation and spindle assembly; Aurora B is a member of the Chromosomal Passenger Complex (CPC) that transfers from the inner centromere in early mitosis to the spindle midzone, equatorial cortex and midbody in late mitosis and cytokinesis. Aurora B functions include regulation of chromosome–microtubule interactions, cohesion, spindle stability and cytokinesis. This review will focus on how interacting proteins make this functional diversity possible by targeting the kinases to different subcellular locations and regulating their activity.

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AIP regulates stability of Aurora-A at early mitotic phase coordinately with GSK-3β

Cited by 17 publications

References 31 publications

PI3-K and GSK-3: Akt-ing together with microtubules

PI3-K and GSK-3: Akt-ing together with microtubules

Glycogen synthase kinase 3B in bovine oocytes and granulosa cells: possible involvement in meiosis during in vitro maturation

Making the Auroras glow: regulation of Aurora A and B kinase function by interacting proteins

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