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Functional differences between L- and T-plastin isoforms.
Arpin, M.; Friederich, Evelyne; Algrain, M. et al.
1994In The Journal of cell biology, 127 (6 Pt 2), p. 1995-2008
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Keywords :
Actin Cytoskeleton/physiology/ultrastructure; Actins/physiology/ultrastructure; Amino Acid Sequence; Animals; Base Sequence; Carrier Proteins/genetics/physiology; Cell Adhesion/physiology; Cell Polarity/physiology; Cells, Cultured; Cytoskeleton/physiology/ultrastructure; Epithelial Cells; Epithelium/ultrastructure; Fibroblasts/cytology/ultrastructure; Humans; Immunohistochemistry; Membrane Glycoproteins; Microfilament Proteins/genetics/physiology; Microvilli/ultrastructure; Molecular Sequence Data; Phosphoproteins/classification/genetics/isolation & purification/physiology; Recombinant Proteins/isolation & purification; Transfection
Abstract :
[en] Fimbrins/plastins are a family of highly conserved actin-bundling proteins. They are present in all eukaryotic cells including yeast, but each isoform displays a remarkable tissue specificity. T-plastin is normally found in epithelial and mesenchymal cells while L-plastin is present in hematopoietic cells. However, L-plastin has been also found in tumor cells of non-hematopoietic origin (Lin, C.-S., R. H. Aebersold, S. B. Kent, M. Varma, and J. Leavitt. 1988. Mol. Cell. Biol. 8:4659-4668; Lin, C.-S., R. H. Aebersold, and J. Leavitt. 1990. Mol. Cell. Biol. 10: 1818-1821). To learn more about the biological significance of their tissue specificity, we have overproduced the T- and L-plastin isoforms in a fibroblast-like cell line, CV-1, and in a polarized epithelial cell line, LLC-PK1. In CV-1 cells, overproduction of T- and L-plastins induces cell rounding and a concomitant reorganization of actin stress fibers into geodesic structures. L-plastin remains associated with microfilaments while T-plastin is almost completely extracted after treatment of the cells with non-ionic detergent. In LLC-PK1 cells, T-plastin induces shape changes in microvilli and remains associated with microvillar actin filaments after detergent extraction while L-plastin has no effect on these structures and is completely extracted. The effect of T-plastin on the organization of microvilli differs from that of villin, another actin-bundling protein. Our experiments indicate that these two isoforms play differing roles in actin filament organization, and do so in a cell type-specific fashion. Thus it is likely that these plastin isoforms play fundamentally different roles in cell function.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Arpin, M.
Friederich, Evelyne ;  University of Luxembourg > Faculty of Science, Technology and Communication (FSTC) > Life Science Research Unit
Algrain, M.
Vernel, F.
Louvard, D.
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Title :
Functional differences between L- and T-plastin isoforms.
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Journal title :
The Journal of cell biology
Volume :
Issue :
6 Pt 2
Pages :
Peer reviewed :
Peer reviewed
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