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WH2 domain: a small, versatile adapter for actin monomers.
Eija Paunola1, Pieta K Mattila, Pekka Lappalainen
1Program in Cellular Biotechnology, Institute of Biotechnology, Viikki Biocenter, P.O. Box 56, University of Helsinki, 00014 Helsinki, Finland.
FEBS Letters
|March 26, 2002
Summary
The WH2 domain is an ancient actin monomer-binding motif found in regulators of the actin cytoskeleton. This motif, present in yeast and animals but not plants, likely predates the split between fungal and animal lineages.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- The actin cytoskeleton is crucial for cellular processes.
- Actin-binding proteins regulate actin structure and dynamics.
- WH2 domain is a conserved actin monomer-binding motif found in various regulators.
Purpose of the Study:
- To investigate the evolutionary history and conservation of the WH2 domain.
- To identify WH2 domain-containing proteins across different species.
- To understand the potential conserved function of WH2 domains in actin monomer binding.
Main Methods:
- Sequence database searches were performed to identify WH2 domain-containing proteins.
- Comparative analysis of WH2 domain sequences and known actin-binding proteins.
Main Results:
- WH2 domain-containing proteins, including WASP, Srv2/CAP, and verprolin/WIP, were identified in yeast and animals.
- No WH2 domain-containing proteins were found in plants.
- Conserved residues in the WH2 domain suggest a conserved mechanism for actin monomer binding.
Conclusions:
- The WH2 domain is an ancient actin monomer-binding motif.
- This motif likely evolved before the divergence of fungal and animal lineages.
- WH2 domains represent a conserved functional unit in actin cytoskeleton regulation across eukaryotes.