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MBC in Press, published online ahead of print June 22, 2005
Mol. Biol. Cell 10.1091/mbc.E05-02-0086

A more recent version of this article appeared on September 1, 2005 Originally published as MBC in Press, 10.1091/mbc.E05-02-0086 on June 27, 2005
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Submitted on February 1, 2005
Revised on June 3, 2005
Accepted on June 9, 2005

A Plasmodium Actin-depolymerizing Factor That Binds Exclusively to Actin Monomers

Herwig Schüler,*{dagger} Ann-Kristin Mueller,{ddagger} and Kai Matuschewski{ddagger}

*Department of Biochemistry and Biophysics, Stockholm University, 10691 Stockholm, Sweden; {ddagger}Department of Parasitology, Heidelberg University School of Medicine, 69120 Heidelberg, Germany

Monitoring Editor: David Drubin

ADF/cofilins (AC) are essential F- and G-actin binding proteins which modulate microfilament turnover. The genome of Plasmodium falciparum, the parasite causing malaria, contains two members of the AC family. Interestingly, P.falciparum ADF1 lacks the F-actin binding residues of the AC consensus. Reverse genetics in the rodent malaria model system suggest that ADF1 performs vital functions during the pathogenic red blood cell stages, whereas ADF2 is not present in these stages. We show that recombinant PfADF1 interacts with monomeric actin but does not bind to actin polymers. While other AC proteins inhibit nucleotide exchange on monomeric actin, the Plasmodium ortholog stimulates nucleotide exchange. Thus PfADF1 differs in its biochemical properties from previously known AC proteins, and seems to promote turnover exclusively by interaction with actin monomers. These findings provide important insights into the low cytosolic abundance and unique turnover characteristics of actin polymers in parasites of the phylum Apicomplexa.

Present address: {dagger}Department of Medical Biochemistry and Biophysics, SGC, Karolinska Institutet, 17177 Stockholm, Sweden.

Address correspondence to: Herwig Schüler (herwig.schuler{at}mbb.ki.se)




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