ArticleThe Journal of cell biology1992
A novel microtubule-binding motif identified in a high molecular weight microtubule-associated protein from Trypanosoma brucei.
Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 51 citations in OpenAlex.
- Novel Cytoskeleton-Associated Proteins inMicroorganisms · 2021Article
- A cytoskeletal protein complex is essential for division of intracellular amastigotes ofThe Journal of biological chemistry · 2020Article
- Regulatory volume decrease in Leishmania mexicana: effect of anti-microtubule drugs.Memorias do Instituto Oswaldo Cruz · 2013Article
- SPM1 stabilizes subpellicular microtubules in Toxoplasma gondii.Eukaryotic cell · 2012Article
- Article
- A novel polymer of tubulin forms the conoid of Toxoplasma gondii.The Journal of cell biology · 2002Article
- Two related subpellicular cytoskeleton-associated proteins in Trypanosoma brucei stabilize microtubules.Molecular biology of the cell · 2002Article
- MHP1, an essential gene in Saccharomyces cerevisiae required for microtubule function.The Journal of cell biology · 1996Article
- Trypanosome variant surface glycoproteins are recognized by self-reactive antibodies in uninfected hosts.Infection and immunity · 1996Article
- Subcellular localization and functional characterization of Nc-p43, a major Neospora caninum tachyzoite surface protein.Infection and immunity · 1996Article
- Tubulin domains for the interaction of microtubule associated protein DMAP-85 from Drosophila melanogaster.Molecular and cellular biochemistry · 1996Article
- The 78,000-M(r) intermediate chain of Chlamydomonas outer arm dynein is a microtubule-binding protein.The Journal of cell biology · 1995Article
- Immunology and morphology studies on the proliferation of in vitro cultivated Echinococcus multilocularis metacestodes.Parasitology research · 1995Article
- Identification and molecular characterization of E-MAP-115, a novel microtubule-associated protein predominantly expressed in epithelial cells.The Journal of cell biology · 1993Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The major component of the cytoskeleton of the parasitic hemoflagellate Trypanosoma brucei is a membrane skeleton which consists of a single layer of tightly spaced microtubules. This array encloses the entire cell body, and it is apposed to, and connected with, the overlying cell membrane. The microtubules of this array contain numerous microtubule-associated proteins. Prominent among those is a family of high molecular weight, repetitive proteins which consist to a large extent of tandemly arranged 38-amino acid repeat units. The binding of one of these proteins, MARP-1, to microtubules has now been characterized in vitro and in vivo. MARP-1 binds to microtubules via tubulin domains other than the COOH-termini used by microtubule-associated proteins from mammalian brain, e.g., MAP2 or Tau. In vitro binding assays using recombinant protein, as well as transfection of mammalian cell lines, have established that the repetitive 38-amino acid repeat units represent a novel microtubule-binding motif. This motif is very similar in length to those of the mammalian microtubule-associated proteins Tau, MAP2, and MAP-U, but both its sequence and charge are different. The observation that the microtubule-binding motifs both of the neural and the trypanosomal proteins are of similar length may reflect the fact that both mediate binding to the same repetitive surface, the microtubule, while their sequence and charge differences are in agreement with the observation that they interact with different domains of the tubulins.
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