PHF20/NF-kB 연구논문이 Nature Communication에 Accept 되었습니다

cell

07-01

축하합니다 허강민 교수님과 공동연구로 진행된 PHF20/NF-kB 연구논문이 최종적으로 Nature Communication에 Accept 되었습니다 (4월13일)

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From: c.schmitt@nature.com [mailto:c.schmitt@nature.com]
Sent: Saturday, April 13, 2013 12:01 AM
Subject: Final revisions for manuscript NCOMMS-12-07030A

Dear Prof Hur,

Your revised manuscript entitled "PHF20 is a novel NF-κB regulator that induces persistent p65 phosphorylation by disrupting recruitment of PP2A to p65 lysine methylation" has now been seen again by our original three referees. The comments of reviewers #1+2 appear below. Reviewer #3 did not submit a formal report but supported publication of your work in the confidential comments to the editor. In the light of their advice I am delighted to say that we are happy, in principle, to publish a suitably revised version in Nature Communications.

We therefore invite you edit your manuscript so that it complies with our format requirements, explained in our checklist for authors at:
http://mts-ncomms.nature.com/letters/NCOMMS_manuscript_checklist.pdf

EDITORIAL REQUESTS:

In addition, we ask that you pay attention to the following points, which will improve the accessibility and therefore the impact of your work:

* Your title was too long (we have a limit of 15 words). I would like to suggest an alternative title, which may also be more concise: "PHF20 regulates NF-κB signalling by disrupting recruitment of PP2A to p65"

* Your abstract was too long (our maximally permitted length is 150 words). I have edited it for length and clarity, and have pasted this alternative version here. Please use this version as a basis for further changes when checking for scientific accuracy and/or completeness:

"Constitutive NF-κB activation in cancer cells is caused by defects in the signalling network responsible for terminating NF-κB activation. Here we report that PHF20 maintains NF-κB in an active state in the nucleus by inhibiting the interaction between PP2A and p65. We show that PHF20 induces canonical NF-κB signaling by increasing the DNA binding activity of NF-κB subunit p65. In PHF20 overexpressing cells, the termination of TNF-induced p65 phosphorylation is impaired whereas upstream signaling events triggered by TNF are unaffected. This effect strictly depends on the interaction between PHF20 and methylated lysine residues of p65, which hinders recruitment of protein phosphatase PP2A to p65, thereby maintaining p65 in a phosphorylated state. We further show that PHF20 levels correlate with p65 phosphorylation levels in human glioma specimens. Our work identifies PHF20 as a novel regulator of NF-κB activation and suggests elevated expression of PHF20 may drive
constitutive NF-κB activation in some cancers such as glioma."


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