Related Experiment Video

Updated: May 19, 2026

Identification of Kinesin-1 Cargos Using Fluorescence Microscopy
08:06

Identification of Kinesin-1 Cargos Using Fluorescence Microscopy

Published on: February 14, 2016

Prion protein impairs kinesin-driven transport

Hanna Nieznanska1, Elzbieta Dudek, Tomasz Zajkowski

  • 1Department of Biochemistry, Nencki Institute of Experimental Biology, 3 Pasteur St., 02-093 Warsaw, Poland.

Biochemical and Biophysical Research Communications
|August 14, 2012
PubMed

Insights

Prion protein (PrP) disrupts cell division by interfering with microtubules and molecular motor function. This study reveals PrP impairs motor protein transport, suggesting a new mechanism for prion-related cell damage.

Area of Science:

  • Cell Biology
  • Neuroscience
  • Biochemistry

Background:

  • Prion protein (PrP) is known to destabilize microtubules by binding to tubulin.
  • PrP interaction with tubulin can lead to tubulin oligomerization and altered microtubule dynamics.
  • Previous research suggests PrP may impact cellular structures involved in cell division.

Purpose of the Study:

  • To investigate the effect of prion protein (PrP) on the function of molecular motors involved in cell division.
  • To determine if PrP binding to microtubules impairs the movement of kinesin motor proteins.
  • To elucidate the mechanism by which PrP cytotoxicity affects microtubule-dependent transport.

Main Methods:

  • Treatment of cells with prion protein (PrP).
  • Microscopy to observe the morphology of mitotic spindles.
  • In vitro assays to measure the binding of Ncd (a kinesin motor) to microtubules in the presence of PrP.
  • Analysis of Ncd-driven microtubule transport.

Main Results:

  • PrP-treated cells displayed abnormal mitotic spindle morphology.
  • Prion protein (PrP) was found to inhibit Ncd-driven microtubule transport.
  • Reduced binding of Ncd to microtubules was observed at low PrP to tubulin ratios.
  • These findings suggest PrP alters microtubule structure, affecting motor protein function.

Conclusions:

  • Prion protein (PrP) not only affects microtubule dynamics but also impairs microtubule-dependent transport by molecular motors.
  • PrP-induced disruption of motor protein function represents a novel mechanism contributing to PrP cytotoxicity.
  • This study highlights the complex interactions between PrP, tubulin, and molecular motors in cellular dysfunction.

More Related Videos

Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis11:09

Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis

Published on: October 30, 2014

Related Concept Videos

The Movement of Organelles and Vesicles01:43

The Movement of Organelles and Vesicles

In eukaryotic cells,  cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...
Microtubule Associated Motor Proteins01:32

Microtubule Associated Motor Proteins

Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they associate with, the direction they move within the cell, and the type of cargo they transport. Motor proteins that associate with microtubules are known as microtubule-associated motor proteins. There are two families of microtubule-associated motor proteins —Kinesins and Dyneins. Both these proteins assist in the transport of cellular cargos...
Energy to Drive Translocation01:37

Energy to Drive Translocation

Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...