The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Class IA phosphoinositide 3-kinases are obligate p85-p110 heterodimers
Open accessAbstract
Class IA phosphoinositide 3-kinases (PI3Ks) signal downstream of tyrosine kinases and Ras and control a wide variety of biological responses. In mammals, these heterodimeric PI3Ks consist of a p110 catalytic subunit (p110α, p110β, or p110δ) bound to any of five distinct regulatory subunits (p85α, p85β, p55γ, p55α, and p50α, collectively referred to as “p85s”). The relative expression levels of p85 and p110 have been invoked to explain key features of PI3K signaling. For example, free (i.e., non-p110-bound) p85α has been proposed to negatively regulate PI3K signaling by competition with p85/p110 for recruitment to phosphotyrosine docking sites. Using affinity and ion exchange chromatography and quantitative mass spectrometry, we demonstrate that the p85 and p110 subunits are present in equimolar amounts in mammalian cell lines and tissues. No evidence for free p85 or p110 subunits could be obtained. Cell lines contain 10,000–15,000 p85/p110 complexes per cell, with p110β and p110δ being the most prevalent catalytic subunits in nonleukocytes and leukocytes, respectively. These results argue against a role of free p85 in PI3K signaling and provide insights into the nonredundant functions of the different class IA PI3K isoforms.
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Absolute quantification of proteins and phosphoproteins from cell lysates by tandem MS
Gerber, S. A., Rush, J., Stemman, O., Kirschner, M. W., & Gygi, S. P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0832254100 · Cited by 1,733
Signalling through Class I PI3Ks in mammalian cells
Hawkins, P. T., Anderson, K. E., Davidson, K., & Stephens, L. R. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340647 · Cited by 540
Critical role for the p110α phosphoinositide-3-OH kinase in growth and metabolic regulation
Foukas, L. C., Claret, M., Pearce, W., Okkenhaug, K., Meek, S., Peskett, E., Sancho, S., Smith, A. J. H., Withers, D. J., & Vanhaesebroeck, B. (2006) · Nature · doi:10.1038/nature04694 · Cited by 463
Self-citationRodriguez-Viciana, P., Sabatier, C., & McCormick, F. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.11.4943-4954.2004 · Cited by 327
Mauvais-Jarvis, F., Ueki, K., Fruman, D. A., Hirshman, M. F., Sakamoto, K., Goodyear, L. J., Iannacone, M., Accili, D., Cantley, L. C., & Kahn, C. R. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0213305 · Cited by 207
Ueki, K., Algenstaedt, P., Mauvais-Jarvis, F., & Kahn, C. R. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.21.8035-8046.2000 · Cited by 148
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Martini, M., De Santis, M. C., Braccini, L., Gulluni, F., & Hirsch, E. (2014) · Annals of Medicine · doi:10.3109/07853890.2014.912836 · Cited by 1,020
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Metadata
- Authors
- Geering, B., Cutillas, P. R., Nock, G., Gharbi, S. I., & Vanhaesebroeck, B.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2007-05-08
- Volume
- 104
- Issue
- 19
- Pages
- 7809-7814
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2046571983
- Cited by
- 225
- References
- 6
- FWCI
- 5.63
- Type
- journal article
- Language
- en
- Open access
- green
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- Geering, B., Cutillas, P. R., Nock, G., Gharbi, S. I., & Vanhaesebroeck, B. (2007). Class IA phosphoinositide 3-kinases are obligate p85-p110 heterodimers. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.0700373104
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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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