The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Phosphoinositide Regulation of the Actin Cytoskeleton
Abstract
▪ Abstract Phosphoinositides [PPIs, which collectively refer to phosphorylated derivatives of phosphatidylinositol (PI)] have a pivotal role as precursors to important second messengers and as bona fide signaling and scaffold targeting molecules. This review focuses on recent advances that elucidate how PPIs, particularly PI(4,5)P2 (PIP 2), directly regulate the actin cytoskeleton in vivo by modulating the activity and targeting of actin regulatory proteins. The role of PIP 2 in stimulating actin polymerization and in establishing cytoskeleton–plasma membrane linkages is emphasized. In addition, the review presents tantalizing evidence that suggests how binding of selected cytoskeletal proteins to membrane PPIs may promote PPI clustering into raft lipid microdomains, alter their accessibility to other proteins, and even distort the bilayer conformation. These actions have profound implications for many other PPI-regulated membrane functions that are beginning to be uncovered, and they suggest how PPIs can mediate crosstalk between the actin cytoskeleton and an expanding spectrum of essential cellular functions.
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Cites
PIP2and Proteins: Interactions, Organization, and Information Flow
McLaughlin, S., Wang, J., Gambhir, A., & Murray, D. (2002) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.31.082901.134259 · Cited by 837
Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex
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Localized Biphasic Changes in Phosphatidylinositol-4,5-Bisphosphate at Sites of Phagocytosis
Botelho, R. J., Teruel, M., Dierckman, R., Anderson, R., Wells, A., York, J. D., Meyer, T., & Grinstein, S. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.7.1353 · Cited by 539
Role of the ENTH Domain in Phosphatidylinositol-4,5-Bisphosphate Binding and Endocytosis
Itoh, T., Koshiba, S., Kigawa, T., Kikuchi, A., Yokoyama, S., & Takenawa, T. (2001) · Science · doi:10.1126/science.291.5506.1047 · Cited by 469
Phospholipid-Cytochrome c Interaction
Tuominen, E. K. J., Wallace, C. J. A., & Kinnunen, P. K. J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200056200 · Cited by 309
Cited by
Phosphoinositides in cell regulation and membrane dynamics
Di Paolo, G., & De Camilli, P. (2006) · Nature · doi:10.1038/nature05185 · Cited by 2,790
Phosphoinositides: Tiny Lipids With Giant Impact on Cell Regulation
Balla, T. (2013) · Physiological Reviews · doi:10.1152/physrev.00028.2012 · Cited by 1,638
Physiology of cell volume regulation in vertebrates
Hoffmann, E. K., Lambert, I. H., & Pedersen, S. F. (2009) · Physiological Reviews · doi:10.1152/physrev.00037.2007 · Cited by 1,441
Shaping cups into phagosomes and macropinosomes
Swanson, J. A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2447 · Cited by 941
Phosphatidylinositol (4,5) bisphosphate regulates HIV-1 Gag targeting to the plasma membrane
Ono, A., Ablan, S. D., Lockett, S. J., Nagashima, K., & Freed, E. O. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405596101 · Cited by 553
Metadata
- Authors
- Yin, H. L., & Janmey, P. A.
- Venue
- Annual Review of Physiology
- Publisher
- Annual Reviews
- Published
- 2003-03
- Volume
- 65
- Issue
- 1
- Pages
- 761-789
- ISSN
- 0066-4278 (ISSN-L)
- 1545-1585
- OpenAlex
- W2123298030
- Cited by
- 660
- References
- 7
- FWCI
- 3.93
- Type
- journal article
- Language
- en
- Open access
- closed
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- Yin, H. L., & Janmey, P. A. (2003). Phosphoinositide Regulation of the Actin Cytoskeleton. Annual Review of Physiology. https://doi.org/10.1146/annurev.physiol.65.092101.142517
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.