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Cited by 425

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

CBP: A Signal-Regulated Transcriptional Coactivator Controlled by Nuclear Calcium and CaM Kinase IV

Chawla, Sangeeta, Hardingham, Giles E., Quinn, David R., Bading, Hilmar·1998·Science

Abstract

Recruitment of the coactivator, CREB binding protein (CBP), by signal-regulated transcription factors, such as CREB [adenosine 3′,5′-monophosphate (cAMP) response element binding protein], is critical for stimulation of gene expression. The mouse pituitary cell line AtT20 was used to show that the CBP recruitment step (CREB phosphorylation on serine-133) can be uncoupled from CREB/CBP–activated transcription. CBP was found to contain a signal-regulated transcriptional activation domain that is controlled by nuclear calcium and calcium/calmodulin–dependent (CaM) protein kinase IV and by cAMP. Cytoplasmic calcium signals that stimulate the Ras mitogen–activated protein kinase signaling cascade or expression of the activated form of Ras provided the CBP recruitment signal but did not increase CBP activity and failed to activate CREB- and CBP-mediated transcription. These results identify CBP as a signal-regulated transcriptional coactivator and define a regulatory role for nuclear calcium and cAMP in CBP-dependent gene expression.

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Metadata

Authors
Chawla, S., Hardingham, G. E., Quinn, D. R., & Bading, H.
Venue
Science
Published
1998-09-04
Volume
281
Issue
5382
Pages
1505-1509
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W1981364887
Cited by
425
References
4
FWCI
12.61
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: CBP: A Signal-Regulated Transcriptional Coactivator Controlled by Nuclear Calcium and CaM Kinase IV. https://app.cochat.ai/papers/10.1126/science.281.5382.1505
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Chawla, S., Hardingham, G. E., Quinn, D. R., & Bading, H. (1998). CBP: A Signal-Regulated Transcriptional Coactivator Controlled by Nuclear Calcium and CaM Kinase IV. Science. https://doi.org/10.1126/science.281.5382.1505

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