The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Inositol-lipid binding motifs: signal integrators through protein-lipid and protein-protein interactions
Abstract
Inositol lipids have emerged as universal lipid regulators of protein signaling complexes in defined membrane compartments. The number of protein modules that are known to recognise these membrane lipids is rapidly increasing. Pleckstrin homology domains, FYVE domains, PX domains, ENTH domains, CALM domains, PDZ domains, PTB domains and FERM domains are all inositide-recognition modules. The latest additions to this list are members of the clathrin adaptor protein and arrestin families. Initially, inositol lipids were believed to recruit signaling molecules to specific membrane compartments, but many of the domains clearly do not possess high enough affinity to act alone as localisation signals. Another important notion is that some (and probably most) of these protein modules also have protein binding partners, and their protein- and lipid-binding activities might influence one another through allosteric mechanisms. Comparison of the structural features of these domains not only reveals a high degree of conservation of their lipid interaction sites but also highlights their evolutionary link to protein modules known for protein-protein interactions. Protein-protein interactions involving lipid-binding domains could serve as the basis for phosphoinositide-induced conformational regulation of target proteins at biological membranes. Therefore, these modules function as crucially important signal integrators, which explains their involvement in a broad range of regulatory functions in eukaryotic cells.
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Citations
Cites
Recognition of Unique Carboxyl-Terminal Motifs by Distinct PDZ Domains
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Curvature of clathrin-coated pits driven by epsin
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A Role for Nuclear Inositol 1,4,5-Trisphosphate Kinase in Transcriptional Control
Odom, A. R., Stahlberg, A., Wente, S. R., & York, J. D. (2000) · Science · doi:10.1126/science.287.5460.2026 · Cited by 394
Disabled‐2 exhibits the properties of a cargo‐selective endocytic clathrin adaptor
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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
Self-citationPhospholipase C–mediated hydrolysis of PIP2 releases ERM proteins from lymphocyte membrane
Hao, J.-J., Liu, Y., Kruhlak, M., Debell, K. E., Rellahan, B. L., & Shaw, S. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200807047 · Cited by 137
Phospholipase D in endocytosis and endosomal recycling pathways
Donaldson, J. G. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.05.011 · Cited by 92
Premkumar, L., Bobkov, A. A., Patel, M., Jaroszewski, L., Bankston, L. A., Stec, B., Vuori, K., Côté, J.-F., & Liddington, R. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.102517 · Cited by 68
Jian, X., Tang, W.-K., Zhai, P., Roy, N. S., Luo, R., Gruschus, J. M., Yohe, M. E., Chen, P.-W., Li, Y., Byrd, R. A., et al. (2015) · Structure · doi:10.1016/j.str.2015.08.008 · Cited by 67
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Metadata
- Authors
- Balla, T.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2005-05-15
- Volume
- 118
- Issue
- 10
- Pages
- 2093-2104
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2072472799
- Cited by
- 253
- References
- 6
- FWCI
- 8.30
- Type
- journal article
- Language
- en
- Open access
- closed
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