AFM force measurements on microtubule‐associated proteins: the projection domain exerts a long‐range repulsive force
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Microtubule‐associated proteins (MAPs) are thought to control spacing between microtubules. We propose that the projection domain is largely unstructured and exerts a long‐range repulsive force that is predominantly entropic in origin, providing a physical mechanism for maintaining spacing. To test this hypothesis, we developed an experimental system where MAPs are electrostatically end‐attached to a flat surface, such that the projection domains extend away from the surface. Atomic force microscopy force measurements on this system show that projection domains exert a long‐range (>100 nm) repulsive force. This force depends on the ionic strength of the solution in a way that is consistent with a polyelectrolyte polymer brush.
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Phosphorylation at the AT8 sites may extend the projection domain outwards from the surface of microtubules and affect mitochondrial transport.
“Phosphorylation at these sites may extend the projection domain outwards from the surface of MTs (Jeganathan et al., 2008) and affect mitochondrial transport (Mukhopadhyay and Hoh, 2001;Jeganathan et al., 2008;Shahpasand 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 Mukhopadhyay and Hoh, 2001
The citation to Mukhopadhyay and Hoh is attached to the mitochondrial-transport clause. In Results and discussion (page unavailable), the paper says MAPs may regulate motor-protein interactions and reports that tau affects motor attachment and detachment, but not transport speed. It does not address mitochondrial transport or link phosphorylation at AT8 sites to a transport effect. (LLM, conf=0.82)
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Research works printed but not linked: 6
- Kreis, T. and Vale, R. (1999) pp. xx, 551, Oxford University Press, Oxford.
- Hyams, J.S. and Lloyd, C.W. (1994) in: Modern Cell Biology (Harford, J.B., Ed.), Vol. 13, Wiley-Liss, New York.
- Black, M.M. (1987) Proc. Natl. Acad. Sci. USA 84, 7783^7787.
- Napper, D.H. (1983) in: Colloid Science, 3, pp. xvi, 428, Aca- demic Press, London.
- Brown, J.R. (1975) Fed. Proc. 34, 591.
- Weingarten, M.D., Lockwood, A.H., Hwo, S.Y. and Kirschner, M.W. (1975) Proc. Natl. Acad. Sci. USA 72, 1858^1862.
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- Authors
- Mukhopadhyay, R., & Hoh, J. H.
- Affiliations
- Johns Hopkins University (US)
- Corresponding author
- Hoh, Jan H.
- ORCID
- Hoh, Jan H.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2001-09-21
- Volume
- 505
- Issue
- 3
- Pages
- 374-378
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2090027894
- Cited by
- 95
- References
- 0
- Citations by year
- 2025: 3 · 2024: 2 · 2023: 3 · 2022: 1 · 2021: 2 · 2019: 3 · 2018: 4 · 2017: 4 · 2016: 6 · 2015: 5 · 2014: 3 · 2013: 5 · 2012: 4
- FWCI
- 1.59
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Force Microscopy Techniques and Applications
- Physical Sciences › Chemistry › Physical and Theoretical Chemistry › Electrostatics and Colloid Interactions
- Keywords
- microtubule-associated proteins, projection domain, entropic force, ionic strength dependence, proteinopathies, electrostatic binding
- MeSH terms
- Animals, Brain Chemistry, Cattle, Microtubule-Associated Proteins, Microscopy, Atomic Force, Entropy, Static Electricity
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