دورية أكاديمية
Phosphoinositide binding inhibits alpha-actinin bundling activity.
العنوان: | Phosphoinositide binding inhibits alpha-actinin bundling activity. |
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المؤلفون: | Fraley, TS, Tran, TC, Corgan, AM, Nash, CA, Hao, J, Critchley, DR, Greenwood, JA |
المصدر: | PubMed ; http://www.ncbi.nlm.nih.gov/pubmedTest/ |
سنة النشر: | 2012 |
المجموعة: | University of Leicester: Leicester Research Archive (LRA) |
مصطلحات موضوعية: | Actin Cytoskeleton, Actinin, Actins, Animals, Binding Sites, Chickens, Dose-Response Relationship, Drug, Fibroblasts, Mutation, Phosphatidylinositols, Protein Binding, Rats, Stress Fibers |
الوصف: | alpha-Actinin is an abundant actin-bundling and adhesion protein that directly links actin filaments to integrin receptors. Previously, in platelet-derived growth factor-treated fibroblasts, we demonstrated that phosphoinositides bind to alpha-actinin, regulating its localization (Greenwood, J. A., Theibert, A. B., Prestwich, G. D., and Murphy-Ullrich, J. E. (2000) J. Cell Biol. 150, 627- 642). In this study, phosphoinositide binding and regulation of alpha-actinin function is further characterized. Phosphoinositide binding specificity, determined using a protein-lipid overlay procedure, suggests that alpha-actinin interacts with phosphates on the 4th and 5th position of the inositol head group. Binding assays and mutational analyses demonstrate that phosphoinositides bind to the calponin homology domain 2 of alpha-actinin. Phosphoinositide binding inhibited the bundling activity of alpha-actinin by blocking the interaction of the actin-binding domain with actin filaments. Consistent with these results, excessive bundling of actin filaments was observed in fibroblasts expressing an alpha-actinin mutant with decreased phosphoinositide affinity. We conclude that the interaction of alpha-actinin with phosphoinositides regulates actin stress fibers in the cell by controlling the extent to which microfilaments are bundled. ; 13905 |
نوع الوثيقة: | article in journal/newspaper |
وصف الملف: | metadata |
اللغة: | English |
تدمد: | 0021-9258 |
العلاقة: | J BIOL CHEM, 2003, 278 (26), pp. 24039-24045; http://hdl.handle.net/2381/14409Test; M213288200 |
DOI: | 10.1074/jbc.M213288200 |
الإتاحة: | https://doi.org/10.1074/jbc.M213288200Test http://hdl.handle.net/2381/14409Test |
رقم الانضمام: | edsbas.2AECAB33 |
قاعدة البيانات: | BASE |
تدمد: | 00219258 |
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DOI: | 10.1074/jbc.M213288200 |