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Stress-induced release of Oct-1 from the nuclear envelope is mediated by JNK phosphorylation of lamin B1

Abstract:

The nuclear lamina can bind and sequester transcription factors (TFs), a function lost if the lamina is abnormal, with missing or mutant lamin proteins. We now show that TF sequestration is not all-or-nothing, but a dynamic physiological response to external signals. We show that the binding of the ubiquitous TF, Oct-1, to lamin B1 was reversed under conditions of cellular stress caused, inter alia, by the chemical methylating agent methylmethanesulfonate (MMS). A search for lamin B1 post-tra...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1371/journal.pone.0177990

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Department:
Oxford, MSD, Pathology Dunn School
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Department:
Oxford, MSD, Pathology Dunn School
More by this author
Department:
Oxford, MSD, Pathology Dunn School
More by this author
Department:
Oxford, MSD, Pathology Dunn School
More by this author
Department:
Lincoln College
Publisher:
Public Library of Science Publisher's website
Journal:
PLoS One Journal website
Volume:
12
Issue:
5
Publication date:
2017-05-24
Acceptance date:
2017-05-06
DOI:
ISSN:
1932-6203
Pubs id:
pubs:695534
URN:
uri:603e2f2f-0573-4cb6-8c61-42d0f1c403d0
UUID:
uuid:603e2f2f-0573-4cb6-8c61-42d0f1c403d0
Local pid:
pubs:695534

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