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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Bakerink, Katelyn J. Crilly, Stephanie E. Speicher, David W. Browder, Kristen C. Khanna, Mansi R. Harper, Sandra L. Mattie, Floyd J. Radyk, Megan D. Thomas, Graham H. |
| Description | Author Affiliation: Khanna MR ( From the Department of Biology and the Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802 and.); Mattie FJ ( From the Department of Biology and the Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802 and.); Browder KC ( From the Department of Biology and the Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802 and.); Radyk MD ( From the Department of Biology and the Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802 and.); Crilly SE ( From the Department of Biology and the Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802 and.); Bakerink KJ ( From the Department of Biology and the Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802 and.); Harper SL ( the Systems Biology Division, The Wistar Institute, Philadelphia, Pennsylvania 19104.); Speicher DW ( the Systems Biology Division, The Wistar Institute, Philadelphia, Pennsylvania 19104.); Thomas GH ( From the Department of Biology and the Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802 and gxt5@psu.edu.) |
| Abstract | The dominant paradigm for spectrin function is that ( ß)2-spectrin tetramers or higher order oligomers form membrane-associated two-dimensional networks in association with F-actin to reinforce the plasma membrane. Tetramerization is an essential event in such structures. We characterize the tetramerization interaction between -spectrin and ß-spectrins in Drosophila. Wild-type -spectrin binds to both ß- and ßH-chains with high affinity, resembling other non-erythroid spectrins. However, -spec(R22S), a tetramerization site mutant homologous to the pathological -spec(R28S) allele in humans, eliminates detectable binding to ß-spectrin and reduces binding to ßH-spectrin â ¼1000-fold. Even though spectrins are essential proteins, -spectrin(R22S) rescues -spectrin mutants to adulthood with only minor phenotypes indicating that tetramerization, and thus conventional network formation, is not the essential function of non-erythroid spectrin. Our data provide the first rigorous test for the general requirement for tetramer-based non-erythroid spectrin networks throughout an organism and find that they have very limited roles, in direct contrast to the current paradigm. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 2 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-01-09 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Cell Membrane Genetics Drosophila Melanogaster Spectrin Actin Cytoskeleton Metabolism Actins Animals Growth & Development Mutation Protein Multimerization Chemistry Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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