T V Satish Tammana

Publications (2)11.12 Total impact

• Article: ADF/cofilin-driven actin dynamics in early events of Leishmania cell division.

  T V Satish Tammana, Amogh A Sahasrabuddhe, Virendra K Bajpai, Chhitar M Gupta
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  ABSTRACT: ADF/cofilin is an actin-dynamics-regulating protein that is required for several actin-based cellular processes such as cell motility and cytokinesis. A homologue of this protein has recently been identified in the protozoan parasite Leishmania, which has been shown to be essentially required in flagellum assembly and cell motility. However, the role of this protein in cytokinesis remains largely unknown. We show here that deletion of the gene encoding ADF/cofilin in these organisms results in several aberrations in the process of cell division. These aberrations include delay in basal body and kinetoplast separation, cleavage furrow progression and flagellar pocket division. In addition to these changes, the intracellular trafficking and actin dynamics are also adversely affected. All these abnormalities are, however, reversed by episomal complementation. Together, these results indicate that actin dynamics regulates early events in Leishmania cell division.
  Journal of Cell Science 06/2010; 123(Pt 11):1894-901. · 6.11 Impact Factor
• Source

  Available from: ias.ac.in

  Article: Actin-depolymerizing factor, ADF/cofilin, is essentially required in assembly of Leishmania flagellum.

  T V Satish Tammana, Amogh A Sahasrabuddhe, Kalyan Mitra, Virendra K Bajpai, Chhitar M Gupta
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  ABSTRACT: ADF/cofilins are ubiquitous actin dynamics-regulating proteins that have been mainly implicated in actin-based cell motility. Trypanosomatids, e.g. Leishmania and Trypanosoma, which mediate their motility through flagellum, also contain a putative ADF/cofilin homologue, but its role in flagellar motility remains largely unexplored. We have investigated the role of this protein in assembly and motility of the Leishmania flagellum after knocking out the ADF/cofilin gene by targeted gene replacement. The resultant mutants were completely immotile, short and stumpy, and had reduced flagellar length and severely impaired beat. In addition, the assembly of the paraflagellar rod was lost, vesicle-like structures were seen throughout the length of the flagellum and the state and distribution of actin were altered. However, episomal complementation of the gene restored normal morphology and flagellar function. These results for the first time indicate that the actin dynamics-regulating protein ADF/cofilin plays a critical role in assembly and motility of the eukaryotic flagellum.
  Molecular Microbiology 10/2008; 70(4):837-52. · 5.01 Impact Factor