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| Citation | Schulze, S.R., Curio-Penny, B., Speese, S., Dialynas, G., Cryderman, D.E., McDonough, C.W., Nalbant, D., Petersen, M., Budnik, V., Geyer, P.K., Wallrath, L.L. (2009). A comparative study of Drosophila and human A-type lamins. PLoS ONE 4(10): e7564. (Export to RIS) | ||
| FlyBase ID | FBrf0208977 | ||
| Publication Type | Research paper | ||
| PubMed ID | 19855837 | ||
| PubMed Abstract | Nuclear intermediate filament proteins, called lamins, form a meshwork that lines the inner surface of the nuclear envelope. Lamins contain three domains: an N-terminal head, a central rod and a C-terminal tail domain possessing an Ig-fold structural motif. Lamins are classified as either A- or B-type based on structure and expression pattern. The Drosophila genome possesses two genes encoding lamins, Lamin C and lamin Dm(0), which have been designated A- and B-type, respectively, based on their expression profile and structural features. In humans, mutations in the gene encoding A-type lamins are associated with a spectrum of predominantly tissue-specific diseases known as laminopathies. Linking the disease phenotypes to cellular functions of lamins has been a major challenge. Drosophila is being used as a model system to identify the roles of lamins in development. Towards this end, we performed a comparative study of Drosophila and human A-type lamins. Analysis of transgenic flies showed that human lamins localize predictably within the Drosophila nucleus. Consistent with this finding, yeast two-hybrid data demonstrated conservation of partner-protein interactions. Drosophila lacking A-type lamin show nuclear envelope defects similar to those observed with human laminopathies. Expression of mutant forms of the A-type Drosophila lamin modeled after human disease-causing amino acid substitutions revealed an essential role for the N-terminal head and the Ig-fold in larval muscle tissue. This tissue-restricted sensitivity suggests a conserved role for lamins in muscle biology. In conclusion, we show that (1) localization of A-type lamins and protein-partner interactions are conserved between Drosophila and humans, (2) loss of the Drosophila A-type lamin causes nuclear defects and (3) muscle tissue is sensitive to the expression of mutant forms of A-type lamin modeled after those causing disease in humans. These studies provide new insights on the role of lamins in nuclear biology and support Drosophila as a model for studies of human laminopathies involving muscle dysfunction. | ||
| DOI | 10.1371/journal.pone.0007564 | ||
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| Language of Publication | English | ||
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| Publication Type | Journal | ||
| Abbreviation | PLoS ONE | ||
| Title | PLoS ONE | ||
| Publication Year | 2006- | ||
| ISBN/ISSN | 1932-6203 | ||
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Data from Reference
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| Constructs (25)
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| Genes (15)
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| Insertions (2)
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| Natural transposons (1)
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