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Department of Biochemistry
Laboratory of Biochemistry of Lipids
Laboratory of Bioenergetics and Biomembranes
Laboratory of Cell Signaling and Metabolic Disorders
Laboratory of Cellular Metabolism
Laboratory of Comparative Enzymology
Laboratory of Intracellular Ion Channels
Laboratory of Molecular Bases of Aging
Laboratory of Molecular Basis of Cell Motilty
Laboratory of Motor Proteins
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nencki.gov.pl » Working Groups » Department of Biochemistry »
Laboratory of Molecular Basis of Cell Motilty


Maria Jolanta RĘDOWICZ

Jolanta JÓŹWIAK, Krzysztof NIEZNAŃSKI, Paweł POMORSKI, Dariusz STĘPKOWSKI,  Magdalena SOBCZAK, Emilia KARCZEWSKA (technician), Serhiy HAVRYLOV (PhD student), Justyna KAROLCZAK (PhD student), Łukasz MAJEWSKI (PhD student), Katarzyna M. OSIECKA (PhD student), Dorota WYPYCH (PhD student)

Research profile

involvement of unconventional myosins, cytoskeletal and adaptor proteins in cell locomotion and intracellular trafficking; structure-function relationships in myosin and actin, the key proteins involved in force generation and motility in both muscle and non-muscle cells; characterization of heterogeneity of prion protein complexes and functional implications of their interaction with microtubules; plasticity of contractile apparatus from skeletal muscle.

Principal techniques: protein chemistry, biochemistry, fluorescence spectroscopy, molecular biology, cell biology (including micromanipulations and in vivo observations); fluorescence and electron microscopy.

Current research activities

  • investigation of involvement of unconventional myosins (in particular of class VI) in cell locomotion and intracellular trafficking of organelles and particles; studies are performed on normal and transformed mammalian and amoebae cells;

  • analysis of subcellular localization and inter-protein interactions of Ruk/CIN85 adaptor protein;

  • investigation of the function of a novel actin-binding protein (ApABP-FI) in Amoeba proteus;

  • probing the interaction of prion protein with microtubular system; elucidation of the mechanism of translocation of prion proteins within the cell;

  • investigation of actin filament dynamics; in particular, effects of ionic strength, the kind of tightly bound divalent cation, and nucleotide n the process of actin polymerization are studied;

  • determining the actin-binding interface on skeletal muscle myosin subfragment 1 in force generating state;

  • analysis of contractile apparatus in normal and denervated muscle subjected to physical training.

Selected publications

Jakubiec-Puka A., Sławińska U., Rędowicz M.J., Biral D., Łapińska I., Chomontowska H., Krawczyk K., Bilski H., Karczewska E., Pliszka B. (2008) Influence of locomotor training on the structure and myosin heavy chains of the denervated rat soleus muscle. Neurological Research, 30, 170-178.

M.J. Rędowicz (2007) Unconventional myosins in muscle. Eur. J. Cell Biol., 86, 549-558.

M. Sobczak, E. Kocik, M.J. Rędowicz (2007) Novel Actin-binding Filamin Immunoanalog with a Coiled-Coil Region in Amoeba proteus. Biochem. Cell Biol., 85, 22-31.

K. Nieznański, Z.A. Podlubnaya, H. Nieznańska (2006) Prion protein inhibits microtubule assembly by inducing tubulin oligomerization. Biochem. Biophys. Res. Commun. 349, 391-399.

B. Wawro, S.Yu. Khaitlina, A. Galińska-Rakoczy, H. Strzelecka-Gołaszewska (2005) Role of actin DNase-I-binding loop in myosin subfragment 1-induced polymerization of G-actin. Implications to the polymerization mechanism. Biophys. J. 88, 2883-2896

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Published at: 2009-02-06 11:32

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