Volume 63, Issue 1 pp. 14-28
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Caenorhabditis elegans expresses three functional profilins in a tissue-specific manner

D. Polet

D. Polet

Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium

Department of Medical Protein Chemistry (VIB09), Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium

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A. Lambrechts

A. Lambrechts

Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium

Department of Medical Protein Chemistry (VIB09), Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium

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K. Ono

K. Ono

Department of Pathology, Emory University, Atlanta, Georgia

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A. Mah

A. Mah

Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada V5A 1S6

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F. Peelman

F. Peelman

Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium

Department of Medical Protein Chemistry (VIB09), Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium

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J. Vandekerckhove

J. Vandekerckhove

Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium

Department of Medical Protein Chemistry (VIB09), Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium

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D. L. Baillie

D. L. Baillie

Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada V5A 1S6

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C. Ampe

Corresponding Author

C. Ampe

Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium

Department of Medical Protein Chemistry (VIB09), Faculty of Medicine and Health Sciences, Ghent University, Ghent, Belgium

Department of Biochemistry, Faculty of Medicine and Health Sciences, Ghent University, A. Baertsoenkaai 3, B-9000 Ghent, BelgiumSearch for more papers by this author
S. Ono

S. Ono

Department of Pathology, Emory University, Atlanta, Georgia

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First published: 29 November 2005
Citations: 30

Abstract

Profilins are actin binding proteins, which also interact with polyphosphoinositides and proline-rich ligands. On the basis of the genome sequence, three diverse profilin homologues (PFN) are predicted to exist in Caenorhabditis elegans. We show that all three isoforms PFN-1, PFN-2, and PFN-3 are expressed in vivo and biochemical studies indicate they bind actin and influence actin dynamics in a similar manner. In addition, they bind poly(L-proline) and phosphatidylinositol 4,5-bisphosphate micelles. PFN-1 is essential whereas PFN-2 and PFN-3 are nonessential. Immunostainings revealed different expression patterns for the profilin isoforms. In embryos, PFN-1 localizes in the cytoplasm and to the cell–cell contacts at the early stages, and in the nerve ring during later stages. During late embryogenesis, expression of PFN-3 was specifically detected in body wall muscle cells. In adult worms, PFN-1 is expressed in the neurons, the vulva, and the somatic gonad, PFN-2 in the intestinal wall, the spermatheca, and the pharynx, and PFN-3 localizes in a striking dot-like fashion in body wall muscle. Thus the model organism Caenorhabditis elegans expresses three profilin isoforms and is the first invertebrate animal with tissue-specific profilin expression. Cell Motil. Cytoskeleton, 2006.© 2005 Wiley-Liss, Inc.

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