Literature summary for 2.7.11.21 extracted from

Klebba, J.E.; Buster, D.W.; McLamarrah, T.A.; Rusan, N.M.; Rogers, G.C.
Autoinhibition and relief mechanism for polo-like kinase 4 (2015), Proc. Natl. Acad. Sci. USA, 112, E657-E666.

Search for more literature for 2.7.11.21

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of full-length Plk4, subcloned into a pMT vector containing an in-frame coding sequence for EGFP or myc and the inducible metallothionein promoter, in Drosophila S2 cells, recombinant expression of the C-terminally FLAG-His6-tagged polo kinase domain of Plk4 in Escherichia coli strain BL21(DE3)	Drosophila melanogaster

Protein Variants

Protein Variants	Comment	Organism
additional information	complete inactivation of a kinase domain mutant. Expression of Plk4 phospho-mutants influences centriole numbers	Drosophila melanogaster
S374A/S378A	site-directed mutagenesis within L1 (GST-L1-Ala-602), the double mutant shows reduced enzyme activity compared to the wild-type enzyme	Drosophila melanogaster

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	Plk4 possesses an autoinhibitory mechanism mediated by a linker (L1) near the kinase domain, newly synthesized Plk4 is autoinhibited by L1. Autoinhibition is a conserved feature of Plks. In the case of Plk4, autoinhibition is relieved after homodimerization and is accomplished by PB3 and by autophosphorylation of L1. In contrast, autophosphorylation of the second linker promotes separation of the Plk4 homodimer. Mechanism for Plk4 autoinhibition, overview	Drosophila melanogaster

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Drosophila melanogaster
Mn2+	required	Drosophila melanogaster

Organism

Organism	UniProt	Comment	Textmining
Drosophila melanogaster	O97143	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	the enzyme performs autophosphorylation. Plk4 phosphorylation pattern, overview	Drosophila melanogaster
ubiquitination	polo box 1, PB1, of Plk4 contains multiple ubiquitination sites. At least some of the Lys in PB1 are physiologically important targets of Plk4 ubiquitination, overview	Drosophila melanogaster

Purification (Commentary)

Purification (Comment)	Organism
recombinant C-terminally FLAG-His6-tagged polo kinase domain of Plk4 fromherichia coli strain BL21(DE3) by nickel affinity chromatography	Drosophila melanogaster

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	autophosphorylation of wild-type full-length enzyme and isolated kinase domain	Drosophila melanogaster	?	-	?

Subunits

Subunits	Comment	Organism
homodimer	the three polo boxes of Plk4 are crucial for Plk4 homodimerization	Drosophila melanogaster

Synonyms

Synonyms	Comment	Organism
for polo-like kinase 4	-	Drosophila melanogaster
PLK4	-	Drosophila melanogaster

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Drosophila melanogaster

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.3	-	assay at	Drosophila melanogaster

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Drosophila melanogaster

General Information

General Information	Comment	Organism
malfunction	kinase activity is impaired in Plk4-DELTAPB3, polo box 3-mutated enzyme, reducing its ability to transautophosphorylate and recruit Slimb and thereby increasing its stability	Drosophila melanogaster
additional information	the three polo boxes of Plk4 not only are crucial for Plk4 homodimerization and ubiquitination but also relieve autoinhibition caused by linker 1. Polo box 3 is required for kinase activity	Drosophila melanogaster
physiological function	polo-like kinase 4 is a master regulator of centriole duplication, and its hyperactivity induces centriole amplification. Homodimeric Plk4 is ubiquitinated as a result of autophosphorylation, promoting its own degradation and preventing centriole amplification. Speculative multistep model for Plk4 activation and regulation, overview	Drosophila melanogaster

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Release 2023.1 (January 2023)