Differential Regulation of Dynein and Kinesin Motor Proteins by Tau

By R. Dixit, J. Ross, Y. Goldman, E. Holzbaur. Science, 2008

1,024 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/2df54b83d48e901161e69b7ef758c1c24912a134

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. R. Vale
2. E. Holzbaur
3. Zu-Hang Sheng
4. E. Mandelkow
5. Qian Cai
6. L. Mucke
7. Alison E. Twelvetrees
8. Debashish Chowdhury

In Molecular Biology

1. E. Mandelkow
2. L. Ittner
3. J. Götz
4. E. Holzbaur
5. Zu-Hang Sheng
6. R. Vale
7. Qian Cai
8. L. Mucke

Citations in the corpus

• Biochemistry and cell biology of tau protein in neurofibrillary degeneration. (2012, background): “Another indirect function is the inhibition of MT-dependent transport by motor proteins, which is based on the competition between motors (kinesin, dynein) and MAPs for binding sites on the MTsurface (Seitz et al. 2002; Stamer et al. 2002; Dixit et al. 2008).”
• Animal models of Alzheimer's disease and frontotemporal dementia (2008, background): “Both tau and APP might be directly involved in axonal transport: tau regulates motor-protein binding to microtubules and APP links motor proteins to cargo”
• Tau mislocalization to dendritic spines mediates synaptic dysfunction independently of neurodegeneration (2010, background): “, 2005; Gendron and Petrucelli, 2009), potentially disrupting kinesin and dynein motor protein function and axonal transport (Mandelkow et al., 2003; Dixit et al., 2008), permitting direct neurotoxic interactions between tau and the actin cytoskeleton (Fulga et al.”
• AXONAL TRANSPORT: CARGO-SPECIFIC MECHANISMS OF MOTILITY AND REGULATION (2014, background): “…that dynein is a less effective motor than kinesin, both the flexible nature of dynein and its ability to move backward and sideways along a microtubule may allow the motor to function effectively in teams (Mallik et al., 2013), and to navigate around obstacles along its path (Dixit et al., 2008b).”
• Alzheimer Disease: An Update on Pathobiology and Treatment Strategies (2019, neutral): “The physiological role of tau in the CNS is not entirely clear, although numerous in vitro experiments have documented important roles in microtubule assembly and stabilization of neuronal axons and regulation of microtubule transport (Dixit et al., 2008; Weingarten et al., 1975).”
• The Many Faces of Tau (2011, background): “Tau can interfere with the binding of motor proteins to microtubules (Dixit et al., 2008; Ebneth et al., 1998), and there is a gradient of tau along the axon; the highest levels are closest to the synapse (Mandell and Banker, 1996).”
• Dendritic function of tau mediates amyloid-beta toxicity in Alzheimer's disease mouse models. (2010, positive): “It is important to note that levels of tau in the dendritic compartment are much lower than in axons, suggesting that under physiological conditions a major function of tau is in axonal MT stabilization and regulation of MT-dependent processes (Dixit et al., 2008; Weingarten et al., 1975).”
• Mitochondrial transport in neurons: impact on synaptic homeostasis and neurodegeneration (2012, background): “The binding of tau to microtubules can reverse the direction in which dynein moves, whereas kinesin tends to detach when moving along tau-decorated microtubule”
• Regulators of the cytoplasmic dynein motor (2009, background): “The variable length and sideways stepping of dynein could allow it to more easily pass obstacles on the microtubule, but whether the stepping behaviour of dynein is in fact modulated in response to its surroundings has not yet been teste”