The Journal of Cell Biology, Vol 91, 175-183, Copyright © 1981 by The Rockefeller University Press

ARTICLES

Two Drosophila melanogaster proteins related to intermediate filament proteins of vertebrate cells

FG Falkner, H Saumweber and H Biessmann

Monoclonal antibodies were prepared against a 46,000 mol wt major cytoplasmic protein from Drosophila melanogaster Kc cells. These antibodies reacted with the 46,000 and a 40,000 mol wt protein from Kc cells. Some antibodies showed cross-reaction with 55,000 (vimentin) and 52,000 mol wt (desmin) proteins from baby hamster kidney (BHK) cells that form intermediate sized filaments in vertebrate cells. In indirect immunofluorescence, the group of cross reacting antibodies stained a filamentous meshwork in the cytoplasm of vertebrate cells. In Kc cells the fluorescence seemed to be localized in a filamentous meshwork that became more obvious after the cells had flattened out on a surface. These cytoskeletal structures are heat-labile; the proteins in Kc or BHK cells rearrange after a brief heat shock, forming juxtanuclear cap structures.
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• Liang, P, MacRae, T. (1997). Molecular chaperones and the cytoskeleton. J. Cell Sci. 110: 1431-1440 [Abstract]  
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• Bossie, C., Sanders, M. (1993). A cDNA from Drosophila melanogaster encodes a lamin C-like intermediate filament protein. J. Cell Sci. 104: 1263-1272 [Abstract]  

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