Phosphorylation of Ataxin-10 by polo-like kinase 1 is required for cytokinesis

Li, Jing; Wang, Jue; Hou, Wenya; Jing, Zhiyi; Tian, Chan; Han, Yi; Liao, Ji; Dong, Meng‐Qiu; Xu, Xingzhi

doi:10.4161/cc.10.17.15922

Cited by 37 publications

(42 citation statements)

References 33 publications

(50 reference statements)

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“…Taken together, our findings identify Plk1 as a novel player within the NPH protein complex and NPHP1 as a novel Plk1 substrate. Interestingly, a novel recently identified NPH-related gene, Ataxin-10, has also been reported to be a substrate of Plk1, although in a mitotic function [56]. Beside the NPHPs, Plk1 might have additional targets within the NPH complex, within the transition zone proteins or the ciliary proteome.…”

Section: Discussionmentioning

confidence: 99%

The Centrosomal Kinase Plk1 Localizes to the Transition Zone of Primary Cilia and Induces Phosphorylation of Nephrocystin-1

et al. 2012

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Polo-like kinase (Plk1) plays a central role in regulating the cell cycle. Plk1-mediated phosphorylation is essential for centrosome maturation, and for numerous mitotic events. Although Plk1 localizes to multiple subcellular sites, a major site of action is the centrosomes, which supports mitotic functions in control of bipolar spindle formation. In G0 or G1 untransformed cells, the centriolar core of the centrosome differentiates into the basal body of the primary cilium. Primary cilia are antenna-like sensory organelles dynamically regulated during the cell cycle. Whether Plk1 has a role in ciliary biology has never been studied. Nephrocystin-1 (NPHP1) is a ciliary protein; loss of NPHP1 in humans causes nephronophthisis (NPH), an autosomal-recessive cystic kidney disease. We here demonstrate that Plk1 colocalizes with nephrocystin-1 to the transition zone of primary cilia in epithelial cells. Plk1 co-immunoprecipitates with NPHP1, suggesting it is part of the nephrocystin protein complex. We identified a candidate Plk1 phosphorylation motif (D/E-X-S/T-φ-X-D/E) in nephrocystin-1, and demonstrated in vitro that Plk1 phosphorylates the nephrocystin N-terminus, which includes the specific PLK1 phosphorylation motif. Further, induced disassembly of primary cilia rapidly evoked Plk1 kinase activity, while small molecule inhibition of Plk1 activity or RNAi-mediated downregulation of Plk1 limited the first and second phase of ciliary disassembly. These data identify Plk1 as a novel transition zone signaling protein, suggest a function of Plk1 in cilia dynamics, and link Plk1 to the pathogenesis of NPH and potentially other cystic kidney diseases.

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Section: Discussionmentioning

confidence: 99%

The Centrosomal Kinase Plk1 Localizes to the Transition Zone of Primary Cilia and Induces Phosphorylation of Nephrocystin-1

et al. 2012

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“…Peptides were extracted sequentially with 5% formic acid (FA)/50% acetonitrile and 0.1% FA/75% acetonitrile, dried under vacuum, then resuspended in 0.1% FA. LC-MS/MS and data analysis were performed as described previously [47] except that the peptide sample was loaded directly on an analytical reverse-phase column.…”

Section: Methodsmentioning

confidence: 99%

Phosphorylation-Coupled Proteolysis of the Transcription Factor MYC2 Is Important for Jasmonate-Signaled Plant Immunity

et al. 2013

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As a master regulator of jasmonic acid (JA)–signaled plant immune responses, the basic helix-loop-helix (bHLH) Leu zipper transcription factor MYC2 differentially regulates different subsets of JA–responsive genes through distinct mechanisms. However, how MYC2 itself is regulated at the protein level remains unknown. Here, we show that proteolysis of MYC2 plays a positive role in regulating the transcription of its target genes. We discovered a 12-amino-acid element in the transcription activation domain (TAD) of MYC2 that is required for both the proteolysis and the transcriptional activity of MYC2. Interestingly, MYC2 phosphorylation at residue Thr328, which facilitates its turnover, is also required for the MYC2 function to regulate gene transcription. Together, these results reveal that phosphorylation-coupled turnover of MYC2 stimulates its transcription activity. Our results exemplify that, as with animals, plants employ an “activation by destruction” mechanism to fine-tune their transcriptome to adapt to their ever-changing environment.

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“…LC-MS/MS analyses of the resulting peptides were carried out on an LTQ-Orbitrap (ThermoFisher Scientific) or LTQ-Orbitrap Velos (ThermoFisher Scientific) as described before with slight modifications (Li et al, 2011). CID MS2 with neutral-loss triggered MS3 spectra were collected on LTQ-Orbitrap and HCD MS2 spectra were collected on LTQ-Orbitrap Velos.…”

Section: Methodsmentioning

confidence: 99%

CAMKII and Calcineurin regulate the lifespan of Caenorhabditis elegans through the FOXO transcription factor DAF-16

Xie

Ding

et al. 2013

eLife

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The insulin-like signaling pathway maintains a relatively short wild-type lifespan in Caenorhabditis elegans by phosphorylating and inactivating DAF-16, the ortholog of the FOXO transcription factors of mammalian cells. DAF-16 is phosphorylated by the AKT kinases, preventing its nuclear translocation. Calcineurin (PP2B phosphatase) also limits the lifespan of C. elegans, but the mechanism through which it does so is unknown. Herein, we show that TAX-6•CNB-1 and UNC-43, the C. elegans Calcineurin and Ca2+/calmodulin-dependent kinase type II (CAMKII) orthologs, respectively, also regulate lifespan through DAF-16. Moreover, UNC-43 regulates DAF-16 in response to various stress conditions, including starvation, heat or oxidative stress, and cooperatively contributes to lifespan regulation by insulin signaling. However, unlike insulin signaling, UNC-43 phosphorylates and activates DAF-16, thus promoting its nuclear localization. The phosphorylation of DAF-16 at S286 by UNC-43 is removed by TAX-6•CNB-1, leading to DAF-16 inactivation. Mammalian FOXO3 is also regulated by CAMKIIA and Calcineurin.DOI: http://dx.doi.org/10.7554/eLife.00518.001

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Phosphorylation of Ataxin-10 by polo-like kinase 1 is required for cytokinesis

Cited by 37 publications

References 33 publications

The Centrosomal Kinase Plk1 Localizes to the Transition Zone of Primary Cilia and Induces Phosphorylation of Nephrocystin-1

The Centrosomal Kinase Plk1 Localizes to the Transition Zone of Primary Cilia and Induces Phosphorylation of Nephrocystin-1

Phosphorylation-Coupled Proteolysis of the Transcription Factor MYC2 Is Important for Jasmonate-Signaled Plant Immunity

CAMKII and Calcineurin regulate the lifespan of Caenorhabditis elegans through the FOXO transcription factor DAF-16

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