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Conservation of the gene structure and membrane-targeting signals of germ cell-specific lamin LIII in amphibians and fish

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Hofemeister,  H.
Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society;

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Weber,  K.
Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society;

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Stick,  R.
Department of Biochemistry and Cell Biology, MPI for biophysical chemistry, Max Planck Society;

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Citation

Hofemeister, H., Kuhn, C., Franke, W. W., Weber, K., & Stick, R. (2002). Conservation of the gene structure and membrane-targeting signals of germ cell-specific lamin LIII in amphibians and fish. European Journal of Cell Biology, 81(2), 51-60.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-F45B-B
Abstract
Targeting of nuclear lamins to the inner nuclear membrane requires CaaX motif-dependent posttranslational isoprenylation and carboxyl methylation. We previously have shown that two variants of lamin LIII (i.e., LIIIa and LIIIb) in amphibian oocytes are generated by alternative splicing and differ greatly in their membrane association. An extra cysteine residue (as a potential palmitoylation site) and a basic cluster in conjunction with the CaaX motif function as secondary targeting signals responsible for stable membrane association of lamin LIIIb. cDNA sequencing and genomic analysis of the zebrafish Danio rerio lamin LIII uncovers a remarkable conservation of the genomic organization and of the two secondary membrane-targeting signals in amphibians and fish. The expression pattern of lamin LIII genes is also conserved between amphibians and fish. Danio lamin LIII is expressed in diplotene oocytes. It is absent from male germ cells but is expressed in Sertoli cells of the testis. In addition, we provide sequence information of the entire coding sequence of zebrafish lamin A, which allows comparison of all major lamins from representatives of the four classes of vertebrates.