ATM and Chk2 kinase target the p53 cofactor Strap.
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ATM and Chk2 kinase target the p53 cofactor Strap. / Adams, Cassandra J; Graham, Anne L; Jansson, Martin; Coutts, Amanda S; Edelmann, Mariola; Smith, Linda; Kessler, Benedikt; La Thangue, Nicholas B.
I: EMBO Reports, 2008.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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TY - JOUR
T1 - ATM and Chk2 kinase target the p53 cofactor Strap.
AU - Adams, Cassandra J
AU - Graham, Anne L
AU - Jansson, Martin
AU - Coutts, Amanda S
AU - Edelmann, Mariola
AU - Smith, Linda
AU - Kessler, Benedikt
AU - La Thangue, Nicholas B
PY - 2008
Y1 - 2008
N2 - The p53 cofactor Strap (stress responsive activator of p300) is directly targeted by the DNA damage signalling pathway where phosphorylation by ATM (ataxia telangiectasia mutated) kinase facilitates nuclear accumulation. Here, we show that Strap regulation reflects the coordinated interplay between different DNA damage-activated protein kinases, ATM and Chk2 (Checkpoint kinase 2), where phosphorylation by each kinase provides a distinct functional consequence on the activity of Strap. ATM phosphorylation prompts nuclear accumulation, which we show occurs by impeding nuclear export, whereas Chk2 phosphorylation augments protein stability once Strap has attained a nuclear location. These results highlight the various functional roles undertaken by the DNA damage signalling kinases in Strap control and, more generally, shed light on the pathways that contribute to the regulation of the p53 response.
AB - The p53 cofactor Strap (stress responsive activator of p300) is directly targeted by the DNA damage signalling pathway where phosphorylation by ATM (ataxia telangiectasia mutated) kinase facilitates nuclear accumulation. Here, we show that Strap regulation reflects the coordinated interplay between different DNA damage-activated protein kinases, ATM and Chk2 (Checkpoint kinase 2), where phosphorylation by each kinase provides a distinct functional consequence on the activity of Strap. ATM phosphorylation prompts nuclear accumulation, which we show occurs by impeding nuclear export, whereas Chk2 phosphorylation augments protein stability once Strap has attained a nuclear location. These results highlight the various functional roles undertaken by the DNA damage signalling kinases in Strap control and, more generally, shed light on the pathways that contribute to the regulation of the p53 response.
U2 - 10.1038/embor.2008.186
DO - 10.1038/embor.2008.186
M3 - Journal article
C2 - 18833288
JO - E M B O Reports
JF - E M B O Reports
SN - 1469-221X
ER -
ID: 7750970