Details der Publikation - Isoform specific phosphorylation of p53 by protein kinase CK1

Isoform specific phosphorylation of p53 by protein kinase CK1

Abstract The ability of three isoforms of protein kinase CK1 (α, $ γ_{1} $, and δ) to phosphorylate the N-terminal region of p53 has been assessed using either recombinant p53 or a synthetic peptide reproducing its 1–28 sequence. Both substrates are readily phosphoylated by CK1δ and CK1α, but not by the γ isoform. Affinity of full size p53 for CK1 is 3 orders of magnitude higher than that of its N-terminal peptide (Km 0.82 μM vs 1.51 mM). The preferred target is S20, whose phosphorylation critically relies on E17, while S6 is unaffected despite displaying the same consensus (E-x-x-S). Our data support the concept that non-primed phosphorylation of p53 by CK1 is an isoform-specific reaction preferentially affecting S20 by a mechanism which is grounded both on a local consensus and on a remote docking site mapped to the $ K^{221} $$ RQK^{224} $ loop according to modeling and mutational analysis..

Medienart:	E-Artikel

Erscheinungsjahr:	2009
Erschienen:	2009

Enthalten in:	Zur Gesamtaufnahme - volume:67
Enthalten in:	Cellular and molecular life sciences - 67(2009), 7 vom: 30. Dez., Seite 1105-1118

Sprache:	Englisch

Beteiligte Personen:	Venerando, Andrea [VerfasserIn] Marin, Oriano [VerfasserIn] Cozza, Giorgio [VerfasserIn] Bustos, Victor H. [VerfasserIn] Sarno, Stefania [VerfasserIn] Pinna, Lorenzo Alberto [VerfasserIn]

Links:	Volltext [lizenzpflichtig]

Themen:	CK1 CKI Casein kinase 1 P53 Ser20 P53 phosphorylation

Anmerkungen:	© Birkhäuser Verlag, Basel/Switzerland 2009

doi:	10.1007/s00018-009-0236-7

funding:
Förderinstitution / Projekttitel:

PPN (Katalog-ID):	OLC2080776800

Internformat


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520			\|a Abstract The ability of three isoforms of protein kinase CK1 (α, $ γ_{1} $, and δ) to phosphorylate the N-terminal region of p53 has been assessed using either recombinant p53 or a synthetic peptide reproducing its 1–28 sequence. Both substrates are readily phosphoylated by CK1δ and CK1α, but not by the γ isoform. Affinity of full size p53 for CK1 is 3 orders of magnitude higher than that of its N-terminal peptide (Km 0.82 μM vs 1.51 mM). The preferred target is S20, whose phosphorylation critically relies on E17, while S6 is unaffected despite displaying the same consensus (E-x-x-S). Our data support the concept that non-primed phosphorylation of p53 by CK1 is an isoform-specific reaction preferentially affecting S20 by a mechanism which is grounded both on a local consensus and on a remote docking site mapped to the $ K^{221} $$ RQK^{224} $ loop according to modeling and mutational analysis.
650		4	\|a Casein kinase 1
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952			\|d 67 \|j 2009 \|e 7 \|b 30 \|c 12 \|h 1105-1118

Isoform specific phosphorylation of p53 by protein kinase CK1

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