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Infect Genet Evol. 2009 Dec;9(6):1275-86. doi: 10.1016/j.meegid.2009.09.001. Epub 2009 Sep 22.

Apicortin, a unique protein, with a putative cytoskeletal role, shared only by apicomplexan parasites and the placozoan Trichoplax adhaerens.

Author information

1
Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, Karolina Ășt 29, H-1113 Budapest, Hungary. orosz@enzim.hu

Abstract

A new protein, termed apicortin, has been identified, which contains a DCX (doublecortin) and a partial p25-alpha domain. The DCX domains of the doublecortin superfamily are responsible for their microtubule binding and stabilizing properties. The p25-alpha domain occurs in TPPPs (Tubulin Polymerization Promoting Proteins) exhibiting Microtubule Associated Protein (MAP)-like functions. TPPP orthologs can be classified as long- and short-type ones. The latter ones do not contain the partial p25-alpha domain, which is the most conservative part of the long-type TPPPs and was evolutionary-preserved independently from the whole domain. Apicortin seems to occur only in the placozoan animal Trichoplax adhaerens and in each of the apicomplexan parasites, the genomes of which are available. The function of the novel protein can be predicted from the fact that it contains two different microtubule-binding domains. Apicomplexans, important pathogens of humans and animals, possess unique cytoskeletal elements, as subpellicular microtubules and apical polar rings, which are specific for this phylum, extremely stabilized by unknown MAPs. One of the candidates can be the apicortin, which is supported by a recent experimental proteomics analysis. The role of the new protein in T. adhaerens may be similar but needs clarification.

PMID:
19778640
DOI:
10.1016/j.meegid.2009.09.001
[Indexed for MEDLINE]

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