Mikolajka, Aleksandra and Yan, Xiumin and Popowicz, Grzegorz M. and Smialowski, Pawel and Nigg, Erich A. and Holak, Tad A.. (2006) Structure of the N-terminal domain of the FOP (FGFR1OP) protein and implications for its dimerization and centrosomal localization. Journal of molecular biology, Vol. 359, H. 4. pp. 863-875.
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Official URL: http://edoc.unibas.ch/dok/A5249351
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Abstract
The fibroblast growth factor receptor 1 (FGFR1) oncogene partner, FOP, is a centrosomal protein that is involved in the anchoring of microtubules (MTS) to subcellular structures. The protein was originally discovered as a fusion partner with FGFR1 in oncoproteins that give rise to stem cell myeloproliferative disorders. A subsequent proteomics screen identified FOP as a component of the centrosome. FOP contains a Lis-homology (LisH) motif found in more than 100 eukaryotic proteins. LisH motifs are believed to be involved in microtubule dynamics and organization, cell migration, and chromosome segregation; several of them are associated with genetic diseases. We report here a 1.6A resolution crystal structure of the N-terminal dimerization domain of FOP. The structure comprises an alpha-helical bundle composed of two antiparallel chains, each of them having five alpha-helices. The central part of the dimer contains the LisH domain. We further determined that the FOP LisH domain is part of a longer N-terminal segment that is required, albeit not sufficient, for dimerization and centrosomal localization of FOP.
Faculties and Departments: | 05 Faculty of Science > Departement Biozentrum 05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Cell Biology (Nigg) |
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UniBasel Contributors: | Nigg, Erich A. |
Item Type: | Article, refereed |
Article Subtype: | Research Article |
Publisher: | Elsevier |
ISSN: | 0022-2836 |
Note: | Publication type according to Uni Basel Research Database: Journal article |
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Last Modified: | 22 Mar 2012 14:19 |
Deposited On: | 22 Mar 2012 13:17 |
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