Head of laboratory

Scientific Staff

PhD Students

Asset 1 f.borys@nencki.edu.pl
Asset 1 s.ahmadi@nencki.edu.pl
Asset 1 z.samsel@nencki.edu.pl
Asset 1 s.majhi@nencki.edu.pl

Research profile

Cilia, the microtubule-based structures, are assembled by nearly all types of cells in the human body. Lack of cilia or their defects lead to disorders called ciliopathies. The primary ciliary dyskinesia, the disorder caused by improper function or loss of motile cilia, affects one in 15 000 individuals. Using free living ciliate Tetrahymena thermophila and mammalian cells as models we perform functional analysis of new proteins that are involved in the reg- ulation of cilia and basal bodies assembly and motile cilia beating. One of our main goals is to decipher the molecular mechanism that regulates cilia beating. To do so we search for new ciliary proteins (we called them “missing links”) that play roles in the transduction of the mechanochemical signals from the central pair complex to the dynein arms. Our group is also investigating a role of the microtubule associated proteins including microtubule severing proteins and microtubule posttranslational modifications in the microtubular cytoskeleton reorganization and in motile cilia assembly.

Current research activities

  • identification and functional analysis of new ciliary proteins using ciliate Tetrahymena thermophila and ciliated mammalian cells as models
  • analysis of the molecular mechanisms that regulate motile cilia beating
  • role of katanin, a microtubule severing protein and tubulin posttranslational modifications in cilia assembly and function
  • identification and functional analysis of regulators of cilia assembly
  • identification and functional analysis of the posttranslational modifications of non-microtubular tubulins
  • identification and role of the new basal body proteins.

Selected publications

Joachimiak E, Jerka-Dziadosz M, Krzemień-Ojak Ł, Wacławek E, Jedynak K, Urbanska P, Brutkowski W, Sas-Nowosielska H, Fabczak H, Gaertig J, Wloga D.(2018) Multiple phosphorylation sites on γ-tubulin are essential and contribute to the biogenesis of basal bodies in Tetrahymena. J Cell Physiol.  IF 2017= 3,92

Urbanska P, Joachimiak E, Bazan R, Fu G, Poprzeczko M, Fabczak H, Nicastro D, Wloga D. (2018) Ciliary proteins Fap43 and Fap44 interact with each other and are essential for proper cilia and flagella beating. Cell Mol Life Sci. IF 2017 = 6,72

Fu G, Wang Q, Phan N, Urbanska P, Joachimiak E, Lin J, Wloga D, Nicastro D. (2018) The I1 dynein-associated tether and tether head complex is a conserved regulator of ciliary motility. Mol Biol Cell. 29(9):1048-1059. IF 2017 = 3,51

Wloga D, Joachimiak E, Fabczak H. (2017) Tubulin Post-Translational Modifications and Microtubule Dynamics. Int J Mol Sci. 18(10). Review. IF 2017 = 4,06

Wloga D, Joachimiak E, Louka P, Gaertig J.(2017) Posttranslational Modifications of Tubulin and Cilia. Cold Spring Harb Perspect Biol. 2017 Jun 1;9(6) IF 2017 = 9,25