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Cited by 142Alzheimer's disease research and treatmentsMicrotubule and mitosis dynamicsCellular Mechanics and Interactions

The proline-rich domain of tau plays a role in interactions with actin

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He, Hai Jin, Wang, Xing Sheng, Pan, Rong, Wang, Dong Liang, Liu, Ming Nan, He, Rong Qiao·2009·BMC Cell Biology
DOI 10.1186/1471-2121-10-81PMC PMC2784441
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Abstract

BACKGROUND: The microtubule-associated protein tau is able to interact with actin and serves as a cross-linker between the microtubule and actin networks. The microtubule-binding domain of tau is known to be involved in its interaction with actin. Here, we address the question of whether the other domains of tau also interact with actin. RESULTS: Several tau truncation and deletion mutants were constructed, namely N-terminal region (tauN), proline-rich domain (tauPRD), microtubule binding domain (tauMTBD) and C-terminal region (tauC) truncation mutants, and microtubule binding domain (tauDeltaMTBD) and proline-rich domain/microtubule binding domain (tauDeltaPRD&MTBD) deletion mutants. The proline-rich domain truncation mutant (tauPRD) and the microtubule binding domain deletion mutant (tauDeltaMTBD) promoted the formation of actin filaments. However, actin assembly was not observed in the presence of the N-terminal and C-terminal truncation mutants. These results indicate that the proline-rich domain is involved in the association of tau with G-actin. Furthermore, results from co-sedimentation, solid phase assays and electron microscopy showed that the proline-rich domain is also capable of binding to F-actin and inducing F-actin bundles. Using solid phase assays to analyze apparent dissociation constants for the binding of tau and its mutants to F-actin resulted in a sequence of affinity for F-actin: tau >> microtubule binding domain > proline-rich domain. Moreover, we observed that the proline-rich domain was able to associate with and bundle F-actin at physiological ionic strength. CONCLUSION: The proline-rich domain is a functional structure playing a role in the association of tau with actin. This suggests that the proline-rich domain and the microtubule-binding domain of tau are both involved in binding to and bundling F-actin.

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  • MAPs bundle actin filaments and cross-link the cellular cytoskeleton formed by microtubules and actin filaments.

    “In addition, MAPs bundle actin filaments and cross-link the cellular cytoskeleton formed by microtubules and actin filaments (Fig. 1a)3–10.”

    From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [4]

    The Results and Discussion show that tau, a microtubule-associated protein, bundles F-actin. The Discussion describes tau and MAP2c as potential cross-linkers between microtubules and actin, but does not establish the citing sentence’s categorical claim that MAPs cross-link those networks in cells. (LLM, conf=0.83)

    Experimental — accuracy not yet measured

  • Interaction of the proline-rich region with F-actin is primarily of electrostatic nature.

    “Interaction with the proline-rich region is primarily of electrostatic nature58.”

    From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [58]

    The Discussion hypothesizes that electrostatic force underlies the interaction between tau’s proline-rich domain and actin, and reports that increasing ionic strength weakens the interaction. The claim presents this proposed mechanism as established and primarily electrostatic, which the paper does not demonstrate. (LLM, conf=0.85)

    Experimental — accuracy not yet measured

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Cited by

Sorted by citations

Authors
He, H. J., Wang, X. S., Pan, R., Wang, D. L., Liu, M. N., & He, R. Q.
Affiliations
Chinese Academy of Sciences (CN)
Corresponding author
He, Rong Qiao
ORCID
He, Rong Qiao
Venue
BMC Cell Biology
Publisher
Springer Science and Business Media LLC
Published
2009-11-08
Volume
10
Issue
1
Pages
81-81
ISSN
1471-2121 (ISSN-L)
DOI
10.1186/1471-2121-10-81
PMC
PMC2784441
OpenAlex
W2019197358
Cited by
142
References
1
Citations by year
2026: 7 · 2025: 7 · 2024: 8 · 2023: 5 · 2022: 10 · 2021: 13 · 2020: 9 · 2019: 11 · 2018: 7 · 2017: 12 · 2016: 7 · 2015: 10 · 2014: 12 · 2013: 3 · 2012: 8
FWCI
4.41
Type
journal article
Language
en
Open access
Licence
Locations
  • BMC Cell Biology (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Institutional Repository of Institute of Psychology, Chinese Academy of Sciences (Institute of Psychology, Chinese Academy of Sciences) (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
Funders
  • National Natural Science Foundation of China (30621004, 2010CB912303)
  • Chinese Academy of Sciences (KSCX2-YW-R, KSCX2-YW-R-119)
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
Keywords
tau protein, proline-rich region, actin binding, F-actin bundling, microtubule-binding domain, F-actin, binding affinity
MeSH terms
Actins, Animals, Humans, Microscopy, Electron, Mutation, Osmolar Concentration, Protein Binding, Rabbits, tau Proteins, Microscopy, Atomic Force, Proline-Rich Protein Domains

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