Asterless is a Polo-like kinase 4 substrate that both activates and inhibits kinase activity depending on its phosphorylation state.

scientific article published on 26 September 2018

Asterless is a Polo-like kinase 4 substrate that both activates and inhibits kinase activity depending on its phosphorylation state. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1091/MBC.E18-07-0445
P932PMC publication ID6249866
P698PubMed publication ID30256714

P2093author name stringNasser M Rusan
Kevin C Slep
Daniel W Buster
Gregory C Rogers
Amy E Byrnes
Jonathan Nye
Cody J Boese
Tiffany A McLamarrah
P2860cites workAsterless is a scaffold for the onset of centriole assemblyQ24300230
Cep152 acts as a scaffold for recruitment of Plk4 and CPAP to the centrosomeQ24306268
The SCF-FBXW5 E3-ubiquitin ligase is regulated by PLK4 and targets HsSAS-6 to control centrosome duplicationQ24310354
Plk4-induced centriole biogenesis in human cellsQ24336451
Genes required for mitotic spindle assembly in Drosophila S2 cellsQ24629513
Multipolar spindle pole coalescence is a major source of kinetochore mis-attachment and chromosome mis-segregation in cancer cellsQ27345177
The Structure of the Plk4 Cryptic Polo Box Reveals Two Tandem Polo Boxes Required for Centriole DuplicationQ27673542
Structural basis for the inhibition of Polo-like kinase 1Q27685281
The PLK4-STIL-SAS-6 module at the core of centriole duplicationQ28071761
A versatile nanotrap for biochemical and functional studies with fluorescent fusion proteinsQ28254176
A mechanism linking extra centrosomes to chromosomal instabilityQ29617923
Expression in aneuploid Drosophila S2 cellsQ33534633
Polo-like kinase 4 kinase activity limits centrosome overduplication by autoregulating its own stabilityQ33618895
The Centrioles, Centrosomes, Basal Bodies, and Cilia of Drosophila melanogaster.Q33642797
Autophosphorylation of polo-like kinase 4 and its role in centriole duplicationQ33647010
Plk4 trans-autophosphorylation regulates centriole number by controlling betaTrCP-mediated degradationQ34118510
GCP6 is a substrate of Plk4 and required for centriole duplicationQ34251767
Cep152 interacts with Plk4 and is required for centriole duplication.Q34317054
Regulation of autophosphorylation controls PLK4 self-destruction and centriole number.Q34382084
Direct interaction of Plk4 with STIL ensures formation of a single procentriole per parental centriole.Q34453657
Cell biology. Reversible centriole depletion with an inhibitor of Polo-like kinase 4.Q34474551
Plk4 phosphorylates Ana2 to trigger Sas6 recruitment and procentriole formationQ34499590
Revisiting the role of the mother centriole in centriole biogenesis.Q34623378
SCFSlimb ubiquitin ligase suppresses condensin II-mediated nuclear reorganization by degrading Cap-H2.Q34636206
The centrosome and its duplication cycleQ35045117
Two Polo-like kinase 4 binding domains in Asterless perform distinct roles in regulating kinase stability.Q35094294
Autoinhibition and relief mechanism for Polo-like kinase 4.Q35128950
Overexpressing centriole-replication proteins in vivo induces centriole overduplication and de novo formation.Q35830134
STIL binding to Polo-box 3 of PLK4 regulates centriole duplicationQ35933358
Structure and function of Polo-like kinasesQ36004636
The Drosophila pericentrin-like protein is essential for cilia/flagella function, but appears to be dispensable for mitosisQ36322473
Conserved molecular interactions in centriole-to-centrosome conversion.Q36480701
Building a centrioleQ36625721
The SCF Slimb ubiquitin ligase regulates Plk4/Sak levels to block centriole reduplication.Q37124885
A centrosome interactome provides insight into organelle assembly and reveals a non-duplication role for Plk4Q37222819
Polo-like kinase 4 autodestructs by generating its Slimb-binding phosphodegronQ37351975
Polo-like kinases: structural variations lead to multiple functionsQ38222354
The SCF/Slimb ubiquitin ligase limits centrosome amplification through degradation of SAK/PLK4.Q38358118
Binding of STIL to Plk4 activates kinase activity to promote centriole assemblyQ38860972
Centrosome Amplification Is Sufficient to Promote Spontaneous Tumorigenesis in MammalsQ38993086
Efficient chromosomal gene modification with CRISPR/cas9 and PCR-based homologous recombination donors in cultured Drosophila cellsQ39002607
Mutagenesis and homologous recombination in Drosophila cell lines using CRISPR/Cas9.Q39044698
Phosphorylation of SAS-6 by ZYG-1 is critical for centriole formation in C. elegans embryosQ39753513
Culture of Drosophila S2 cells and their use for RNAi-mediated loss-of-function studies and immunofluorescence microscopyQ39995047
Phosphorylation of threonine 210 and the role of serine 137 in the regulation of mammalian polo-like kinaseQ40703602
Over-expression of Plk4 induces centrosome amplification, loss of primary cilia and associated tissue hyperplasia in the mouse.Q41868756
Plk4-dependent phosphorylation of STIL is required for centriole duplication.Q42015542
PLK4 trans-Autoactivation Controls Centriole Biogenesis in Space.Q47604754
PLK4 phosphorylation of CP110 is required for efficient centriole assembly.Q50968843
A homeostatic clock sets daughter centriole size in flies.Q52676506
An ordered pattern of Ana2 phosphorylation by Plk4 is required for centriole assembly.Q52678420
Transient PLK4 overexpression accelerates tumorigenesis in p53-deficient epidermis.Q52901124
Prevalence and Significance of the Product Inhibition of EnzymesQ59066805
Bimodal Binding of STIL to Plk4 Controls Proper Centriole Copy NumberQ89091467
P4510describes a project that usesImageJQ1659584
P433issue23
P304page(s)2874-2886
P577publication date2018-09-26
P1433published inMolecular Biology of the CellQ2338259
P1476titleAsterless is a Polo-like kinase 4 substrate that both activates and inhibits kinase activity depending on its phosphorylation state.
P478volume29

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