The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Paxillin comes of age
Open accessAbstract
Paxillin is a multi-domain scaffold protein that localizes to the intracellular surface of sites of cell adhesion to the extracellular matrix. Through the interactions of its multiple protein-binding modules, many of which are regulated by phosphorylation, paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. In particular, paxillin plays a central role in coordinating the spatial and temporal action of the Rho family of small GTPases, which regulate the actin cytoskeleton, by recruiting an array of GTPase activator, suppressor and effector proteins to cell adhesions. When paxillin was first described 18 years ago, the amazing complexity of cell-adhesion organization, dynamics and signaling was yet to be realized. Herein we highlight our current understanding of how the multiple protein interactions of paxillin contribute to the coordination of cell-adhesion function.
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Cites
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Taking Cell-Matrix Adhesions to the Third Dimension
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Angiotensin II cell signaling: physiological and pathological effects in the cardiovascular system
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Unconventional Rac-GEF activity is mediated through the Dock180–ELMO complex
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A truncated isoform of the PP2A B56 subunit promotes cell motility through paxillin phosphorylation
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“Journal of Cell Science 121 (15) NCK 118 PY PY LIM1 LIM2 LIM3 LIM4LD2 LD3 LD5LD4LD1 31 Focal-adhesion targeting PY PY PTP-PEST PAK GITPIX FAK and Src kinases Rac1 Cell adhesion or integrin signaling PS 273 PP2A Localized lamellipodium formation Dephosphorylation Paxillin Fig.”
BackgroundInfluential
Cited by
Focal adhesion kinase: switching between GAPs and GEFs in the regulation of cell motility.
Tomar, A., & Schlaepfer, D. D. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.05.006 · Cited by 223
Calvo, F., Ranftl, R., Hooper, S., Farrugia, A. J., Moeendarbary, E., Bruckbauer, A., Batista, F., Charras, G., & Sahai, E. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.11.052 · Cited by 142
Kumar, G. R., Shum, L., & Glaunsinger, B. A. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05402-11 · Cited by 71
Nemo‐like kinase is involved in NGF‐induced neurite outgrowth via phosphorylating MAP1B and paxillin
Ishitani, T., Ishitani, S., Matsumoto, K., & Itoh, M. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06400.x · Cited by 44
Qu, H., Tu, Y., Guan, J.-L., Xiao, G., & Wu, C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.580811 · Cited by 43
Runx3 inhibits melanoma cell migration through regulation of cell shape change
Zhang, X., Wang, L., Zeng, X., Fujita, T., & Liu, W. (2017) · Cell Biology International · doi:10.1002/cbin.10824 · Cited by 9
Metadata
- Authors
- Deakin, N. O., & Turner, C. E.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2008-08-01
- Volume
- 121
- Issue
- 15
- Pages
- 2435-2444
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2108770100
- Cited by
- 498
- References
- 6
- FWCI
- 15.85
- Type
- journal article
- Language
- en
- Open access
- bronze
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
