Head: Andrzej A. Kasprzak



2013 Professor of Biological Sciences, nomination by the President of the Republic of Poland, Nencki Institute of Experimental Biology, PAS

1997 DSc Habil, Nencki Institute of Experimental Biology, PAS

1979 PhD in Chemistry, Wroclaw University of Science and Technology

1971 MSc in Physical Chemistry, Wroclaw University of Science and Technology


Research trainings:

1980-1981 University of Illinois at Urbana-Champaign, Department of Biochemistry, USA, Prof. Gregorio Weber


Professional employments:

2013 Professor, Nencki Institute of Experimental Biology, PAS

1998-present Head of the Laboratory of Motor Proteins, Nencki Institute of Experimental Biology, PAS

1992-1997 Chargé de Recherche 1ère Classe; Centre National de la Recherche Scientifque, CRBM, Montpellier, France

1984-1989 Research Assistant Professor, University of California, San Francisco, USA


Honors and fellowships:

2010 Polish Academy of Sciences Award for scientific achievements of the team led by Andrzej A. Kasprzak

Staff: Beata Kliszcz (PhD student), Katarzyna Mańko


Research profile:

Molecular motors are systems of one or several molecules, which are capable of cyclically converting chemical energy derived from adenosine triphosphate (ATP) hydrolysis into mechanical work. The generation of movement takes place when the motor molecule is bound to an elongated polymer such as microtubule or actin. While the structure and function of the motor is clearly fundamental, the role of the 'tracks' on which the motors carry their cargoes is also important. The cellular functions of the microtubule do not depend only on the overall polymer structure but to a large extent on the local post-translational modifi- cation of tubulin. These modifications are detected and decoded by motor proteins, MAPS, and other proteins whose properties are changed when a particular modification is detected. The whole process constitutes a general and powerful cellular regulatory mechanism and has been named the "tubulin code". Our work is focused on the molecular mechanisms by which molecular motors recognize and use the information embedded in the microtubules.

Current research activities:

Often a kinesin's-1 cargo is another microtubule, therefore, in this case, the motor generates microtubule-microtubule sliding. There are some indications that the sliding between the microtubules is regulated by post-translational tubulin modification. The microtubule- microtubule movement generated by kinesin-1 occurs in many cellular processes and was observed in live cells. In Drosophila neurons, it was demonstrated that kinesin-1 mediates the sliding. But the factors contributing to this process were never examined. Therefore, the focus of our research is to study the effect of post-translational modification on kinesin- generated sliding movement between two microtubules in vitro and in mammalian neurons. To achieve these goals we combine protein engineering with classical biochemistry and high-resolution imaging techniques such as TIRF microscopy.

Selected publications:

Szczęsna E., Kasprzak A.A. (2012) The C-terminus of kinesin-14 Ncd is a crucial component of the force generating mechanism. FEBS Letters, 586: 854-858.


Braun M., Lansky Z., Bajer S., Fink G., Kasprzak A.A., Diez S. (2013) The  human  kinesin-14  HSET tracks the tips of growing microtubules in vitro. Cytoskeleton, 70: 515-521.


Nitzsche B., Vilfan A., Dudek E., Hajdo L., Kasprzak A.A., Diez S. (2016) The working stroke of the kinesin-14, ncd, comprises at least two substeps of different direction. Proc Natl Acad Sci USA, 113(43): E6582-E6589.


Szczęsna E., Kasprzak A.A. (2016) Insights into the process of EB1-dependent tip-tracking of kinesin-14 Ncd. The role of the microtubule. Eur J Cell Biol, 95(12): 521–530.


Szkop M., Kliszcz B., Kasprzak A. A. (2018) A simple and reproducible protocol of glass surface silanization for TIRF microscopy imaging. Anal Biochem. 549: 119-123.