The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1
Open accessAbstract
Recruitment of p300/CBP by the hypoxia-inducible factor, HIF-1, is essential for the transcriptional response to hypoxia and requires an interaction between the p300/CBP CH1 region and HIF-1α. A new p300-CH1 interacting protein, p35srj, has been identified and cloned. p35srj is an alternatively spliced isoform of MRG1, a human protein of unknown function. Virtually all endogenous p35srj is bound to p300/CBP in vivo, and it inhibits HIF-1 transactivation by blocking the HIF-1α/p300 CH1 interaction. p35srj did not affect transactivation by transcription factors that bind p300/CBP outside the CH1 region. Endogenous p35srj is up-regulated markedly by the HIF-1 activators hypoxia or deferoxamine, suggesting that it could operate in a negative-feedback loop. In keeping with this notion, a p300 CH1 mutant domain, defective in HIF-1 but not p35srj binding, enhanced endogenous HIF-1 function. In hypoxic cells, p35srj may regulate HIF-1 transactivation by controlling access of HIF-1α to p300/CBP, and may keep a significant portion of p300/CBP available for interaction with other transcription factors by partially sequestering and functionally compartmentalizing cellular p300/CBP.
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Cites
Cellular and developmental control of O 2 homeostasis by hypoxia-inducible factor 1α
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Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP
Petrif, F., Giles, R. H., Dauwerse, H. G., Saris, J. J., Hennekam, R. C. M., Masuno, M., Tommerup, N., van Ommen, G.-J. B., Goodman, R. H., Peters, D. J. M., et al. (1995) · Nature · doi:10.1038/376348a0 · Cited by 1,217
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A family of transcriptional adaptor proteins targeted by the E1A oncoprotein
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Self-citationKallio, P. J., Pongratz, I., Gradin, K., McGuire, J., & Poellinger, L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.11.5667 · Cited by 415
p300/MDM2 complexes participate in MDM2-mediated p53 degradation
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Cited by
Hypoxia — a key regulatory factor in tumour growth
Harris, A. L. (2002) · Nature Reviews Cancer · doi:10.1038/nrc704 · Cited by 5,177
Intrinsically unstructured proteins and their functions
Dyson, H. J., & Wright, P. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1589 · Cited by 3,871
Regulation of Mammalian O 2 Homeostasis by Hypoxia-Inducible Factor 1
Semenza, G. L. (1999) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.15.1.551 · Cited by 1,914
HIF-1: mediator of physiological and pathophysiological responses to hypoxia
Semenza, G. L. (2000) · Journal of Applied Physiology · doi:10.1152/jappl.2000.88.4.1474 · Cited by 1,822
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Metadata
- Authors
- Bhattacharya, S., Michels, C. L., Leung, M.-K., Arany, Z. P., Kung, A. L., & Livingston, D. M.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 1999-01-01
- Volume
- 13
- Issue
- 1
- Pages
- 64-75
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2125887885
- Cited by
- 395
- References
- 7
- Type
- posted content
- Language
- en
- Open access
- diamond
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- Bhattacharya, S., Michels, C. L., Leung, M.-K., Arany, Z. P., Kung, A. L., & Livingston, D. M. (1999). Functional role of p35srj, a novel p300/CBP binding protein, during transactivation by HIF-1. Genes & Development. https://doi.org/10.1101/gad.13.1.64
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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