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Differential Regulation of Dynein and Kinesin Motor Proteins by Tau
Open accessAbstract
Dynein and kinesin motor proteins transport cellular cargoes toward opposite ends of microtubule tracks. In neurons, microtubules are abundantly decorated with microtubule-associated proteins (MAPs) such as tau. Motor proteins thus encounter MAPs frequently along their path. To determine the effects of tau on dynein and kinesin motility, we conducted single-molecule studies of motor proteins moving along tau-decorated microtubules. Dynein tended to reverse direction, whereas kinesin tended to detach at patches of bound tau. Kinesin was inhibited at about a tenth of the tau concentration that inhibited dynein, and the microtubule-binding domain of tau was sufficient to inhibit motor activity. The differential modulation of dynein and kinesin motility suggests that MAPs can spatially regulate the balance of microtubule-dependent axonal transport.
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In the citing paper
“Tau impedes kinesin and dynein motors on microtubules via competition for microtubule binding (198); thus tau may also block proper trafficking and fusion of autophagosomes to lysosomes, causing impaired autophagy.”
From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [198]
In the citing paper
“While some motors, such as kinesin-1 and kinesin-3, are strongly inhibited by tau in an isoform- and lattice-dependent manner, others, like kinesin-2 and dynein, can more effectively navigate tau-decorated regions”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Tau envelopes act as selective, reversible barriers along microtubules, regulating the access of motor proteins and other MAPs to the microtubule.”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“The extent of tau’s influence on motor proteins depends on several factors including (1) the tau isoform and PTMs, (2) the underlying microtubule lattice, and (3) the intrinsic properties of the motors themselves.”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Envelope formation is sensitive to the intramolecular lattice spacing between α and β tubulin.”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Tau exhibits both diffusive and cooperative interactions with microtubules.”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Tau does not form envelopes on GMPCPP-polymerized microtubules, which are irreversibly expanded, mimicking the GTP-state, but readily forms envelopes on compacted GDP-lattices or reversibly expanded taxol-lattices”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Tau regulates the axonal cytoskeleton (Kanai et al., 1992; Chen et al., 1992; Panda et al., 2003; Rosenberg et al., 2008; Chung et al., 2015; Biswas and Kalil, 2018), and acts as a selective barrier on microtubules to direct intracellular transport”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Cooperativity leads to cohesive envelope-like structures (Dixit et al., 2008; Hinrichs et al., 2012; McVicker et al., 2014; Siahaan et al., 2019; Tan et al., 2019; Siahaan et al., 2022).”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Axonal cargoes are transported by teams of motors with differing sensitivities to tau, as we observed for kinesin-1 (KIF5C) and kinesin-3 (KIF1A) (Figure 3) and as shown previously”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Previous studies showed that tau differentially regulates motor proteins, with kinesin-1 and kinesin-3 being more sensitive to tau-mediated inhibition than kinesin-2 and dynein”
From Tau hyperphosphorylation impairs cooperative binding to microtubules and perturbs organelle trafficking in neurons (2026) · cites this paper as Dixit et al., 2008
In the citing paper
“Overexpression of either Tau WT, 3A, or 3D reduced anterograde movement of mitochondria in PC12 cells and cortical neurons, as reported (Mandelkow et al., 2004;Hollenbeck and Saxton, 2005;Dixit et al., 2008).”
From Regulation of Mitochondrial Transport and Inter-Microtubule Spacing by Tau Phosphorylation at the Sites Hyperphosphorylated in Alzheimer's Disease (2012) · cites this paper as Dixit et al., 2008
In the citing paper
“Tau is highly expressed in neurons in the mammalian brain, and normally localizes predominantly to axons as an important regulator of axonal transport [124–126].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [124]
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Self-citationMicrotubule orientation and spacing within bundles is critical for long‐range kinesin‐1 motility
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Metadata
- Authors
- Dixit, R., Ross, J. L., Goldman, Y. E., & Holzbaur, E. L. F.
- Affiliations
- University of Pennsylvania (US)
- Corresponding author
- Ross, Jennifer L.
- Holzbaur, Erika L. F.
- Venue
- Science
- Published
- 2008-02-22
- Volume
- 319
- Issue
- 5866
- Pages
- 1086-1089
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC2866193
- OpenAlex
- W1981662243
- Cited by
- 1,012
- References
- 20
- Citations by year
- 2026: 32 · 2025: 35 · 2024: 39 · 2023: 52 · 2022: 68 · 2021: 80 · 2020: 76 · 2019: 59 · 2018: 58 · 2017: 62 · 2016: 52 · 2015: 44 · 2014: 63 · 2013: 42 · 2012: 83
- FWCI
- 24.20
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (5p01ar051174-05)
- National Institute of General Medical Sciences (GM-48661, R01GM048661)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (P01-AR-051174)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
- Keywords
- tau protein, dynein, kinesin, motor proteins, microtubule-associated proteins, axonal transport, microtubule-binding domain, motor protein motility, single-molecule tracking
- MeSH terms
- Alzheimer Disease, Animals, Axonal Transport, Dyneins, Mice, Transgenic, Microscopy, Fluorescence, Microtubules, Models, Neurological, Neurons, Protein Binding, Recombinant Fusion Proteins, Kinesins, tau Proteins, Protein Isoforms, Mice
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