Caenorhabditis elegans expresses three functional profilins in a tissue-specific manner
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
Search for more papers by this authorA. 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
Search for more papers by this authorK. Ono
Department of Pathology, Emory University, Atlanta, Georgia
Search for more papers by this authorA. Mah
Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada V5A 1S6
Search for more papers by this authorF. 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
Search for more papers by this authorJ. 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
Search for more papers by this authorD. L. Baillie
Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada V5A 1S6
Search for more papers by this authorCorresponding 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 authorS. Ono
Department of Pathology, Emory University, Atlanta, Georgia
Search for more papers by this authorD. 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
Search for more papers by this authorA. 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
Search for more papers by this authorK. Ono
Department of Pathology, Emory University, Atlanta, Georgia
Search for more papers by this authorA. Mah
Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada V5A 1S6
Search for more papers by this authorF. 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
Search for more papers by this authorJ. 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
Search for more papers by this authorD. L. Baillie
Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada V5A 1S6
Search for more papers by this authorCorresponding 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 authorS. Ono
Department of Pathology, Emory University, Atlanta, Georgia
Search for more papers by this authorAbstract
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.
Supporting Information
The supplemental materials described in this article can be found at http://www.interscience.wiley.com/jpages/0886-1544/suppmat
Filename | Description |
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jws-cm.20102.lgd-cit.doc55 KB | Supporting Information file jws-cm.20102.lgd-cit.doc |
jws-cm.20102.fig1.doc19.5 KB | Amino acid sequence alignments of profilins from different species. |
jws-cm.20102.fig2.tif10.2 MB | An unrooted consensus Maximum Parsimony phylogenetic tree of profilins calculated with PROTPARS with 100 bootstraps. |
jws-cm.20102.fig3.doc32 KB | A schematic overview on the exon-intron structure of theC. elegans pfngenes and a table with additional genomic information on these genes. |
jws-cm.20102.fig4.tif12.6 MB | Structural models of theC. elegansprofilin isoforms. |
Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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