Cellular and Molecular Life Sciences

, Volume 71, Issue 16, pp 3139–3150

Transport and diffusion of Tau protein in neurons

Review

DOI: 10.1007/s00018-014-1610-7

Cite this article as:
Scholz, T. & Mandelkow, E. Cell. Mol. Life Sci. (2014) 71: 3139. doi:10.1007/s00018-014-1610-7

Abstract

In highly polarized and elongated cells such as neurons, Tau protein must enter and move down the axon to fulfill its biological task of stabilizing axonal microtubules. Therefore, cellular systems for distributing Tau molecules are needed. This review discusses different mechanisms that have been proposed to contribute to the dispersion of Tau molecules in neurons. They include (1) directed transport along microtubules as cargo of tubulin complexes and/or motor proteins, (2) diffusion, either through the cytosolic space or along microtubules, and (3) mRNA-based mechanisms such as transport of Tau mRNA into axons and local translation. Diffusion along the microtubule lattice or through the cytosol appear to be the major mechanisms for axonal distribution of Tau protein in the short-to-intermediate range over distances of up to a millimetre. The high diffusion coefficients ensure that Tau can distribute evenly throughout the axonal volume as well as along microtubules. Motor protein-dependent transport of Tau dominates over longer distances and time scales. At low near-physiological levels, Tau is co-transported along with short microtubules from cell bodies into axons by cytoplasmic dynein and kinesin family members at rates of slow axonal transport.

Keywords

Alzheimer disease Tau protein Diffusion Axonal transport Kinesin Dynein Motor protein Microtubules 

Abbreviations

3′UTR

3′ Untranslated region

aa

Amino acids

CNS

Central nervous system

FRAP

Fluorescence recovery after photobleaching

FTDP17

Fronto-temporal dementia and Parkinsonism linked to chromosome 17

JIP1

c-Jun N-terminal kinase-interacting protein 1

MAP

Microtubule-associated protein

PARPs

Periaxoplasmic ribosomal plaques

PHF

Paired helical filaments

PP1

Protein phosphatase 1

RNP

Ribonucleoprotein

TIRF

Total internal reflection fluorescence

Copyright information

© Springer Basel 2014

Authors and Affiliations

  1. 1.Institute for Molecular and Cell PhysiologyHannover Medical SchoolHannoverGermany
  2. 2.DZNE, German Center for Neurodegenerative DiseasesBonnGermany
  3. 3.CAESAR Research CenterBonnGermany