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Mol Biochem Parasitol ; 136(2): 149-56, 2004 Aug.
Article in English | MEDLINE | ID: mdl-15478794

ABSTRACT

The TGF-beta family of receptor serine/threonine kinases (RSTKs) is responsible for a diverse array of functions in metazoans. Here, we describe the isolation of SmRK2, a type II RSTK expressed in schistosomula and adult stages of Schistosoma mansoni. Based on amino acid sequence homology, SmRK2 is most closely related to the Activin type II receptor subset of RSTKs. SmRK2 appears to be expressed as three different transcripts: one encoding a full-length receptor with 5'- and 3'-untranslated regions (UTRs) (SmRK2), a second encoding a longer form containing no 3'-UTR and no stop codon (SmRK2a), and a third truncated variant (SmRK2b), which contains sequence encoding the first 53 amino acids of the N-terminal extracellular domain followed by an inserted 10 residue hydrophobic domain. Using an anti-peptide antibody raised against a partial extracellular domain sequence common to all three isoforms, SmRK2 was localized predominantly to the tegumental surface of the parasites. We hypothesize that SmRK2 is the receptor partner for the previously reported type I RSTK SmRK1 (or SmTbetaR1) and that together these proteins constitute a receptor system for receiving signals from the mammalian host.


Subject(s)
Protein Serine-Threonine Kinases/genetics , Schistosoma mansoni/enzymology , Schistosoma mansoni/genetics , Amino Acid Sequence , Animals , Base Sequence , Cloning, Molecular , DNA, Complementary/genetics , DNA, Helminth/genetics , Female , Gene Expression , Genes, Helminth , Helminth Proteins/chemistry , Helminth Proteins/genetics , Male , Molecular Sequence Data , Phylogeny , Protein Serine-Threonine Kinases/chemistry , Receptors, Cell Surface/chemistry , Receptors, Cell Surface/genetics , Sequence Homology, Amino Acid
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