ArticleMolecular biology of the cell2000
Functional elements within the dynein microtubule-binding domain.
Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
28 citing papers in PubMed, 90 citations in OpenAlex.
- Long-range electrostatic interactions significantly modulate the affinity of dynein for microtubules.Biophysical journal · 2022Article
- Setting the dynein motor in motion: New insights from electron tomography.The Journal of biological chemistry · 2019Review
- Article
- Cryo-EM of dynein microtubule-binding domains shows how an axonemal dynein distorts the microtubule.eLife · 2019Article
- E-hooks provide guidance and a soft landing for the microtubule binding domain of dynein.Scientific reports · 2018Article
- Peptides mediating DNA transport on microtubules and their impact on non-viral gene transfer efficiency.Bioscience reports · 2017Review
- The calcium-binding protein ALG-2 regulates protein secretion and trafficking via interactions with MISSL and MAP1B proteins.The Journal of biological chemistry · 2017Article
- Near-atomic cryo-EM structure of PRC1 bound to the microtubule.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Cytoplasmic dynein binding, run length, and velocity are guided by long-range electrostatic interactions.Scientific reports · 2016Article
- A flipped ion pair at the dynein-microtubule interface is critical for dynein motility and ATPase activation.The Journal of cell biology · 2015Article
- Article
- Cytoplasmic dynein: tension generation on microtubules and the nucleus.Cellular and molecular bioengineering · 2013Article
- Structural basis for microtubule binding and release by dynein.Science (New York, N.Y.) · 2012Article
- Distinct roles of c-Jun N-terminal kinase isoforms in neurite initiation and elongation during axonal regeneration.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- A low affinity ground state conformation for the Dynein microtubule binding domain.The Journal of biological chemistry · 2010Article
- Communication between the AAA+ ring and microtubule-binding domain of dynein.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2010Review
- Structure and functional role of dynein's microtubule-binding domain.Science (New York, N.Y.) · 2008Article
- The dynein stalk head, the microtubule binding-domain of dynein: NMR assignment and ligand binding.Journal of biomolecular NMR · 2008Article
- Article
- The coordination of cyclic microtubule association/dissociation and tail swing of cytoplasmic dynein.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Dynein interacts with microtubules through an ATP-sensitive linkage mapped to a structurally complex region of the heavy chain following the fourth P-loop motif. Virtually nothing is known regarding how binding affinity is achieved and modulated during ATP hydrolysis. We have performed a detailed dissection of the microtubule contact site, using fragment expression, alanine substitution, and peptide competition. Our work identifies three clusters of amino acids important for the physical contact with microtubules; two of these fall within a region sharing sequence homology with MAP1B, the third in a region just downstream. Amino acid substitutions within any one of these regions can eliminate or weaken microtubule binding (KK3379, 80, E3385, K3387, K3397, KK3410,11, W3414, RKK3418-20, F3426, R3464, S3466, and K3467), suggesting that their activities are highly coordinated. A peptide that actively displaces MAP1B from microtubules perturbs dynein binding, supporting previous evidence for similar sites of interaction. We have also identified four amino acids whose substitutions affect release of the motor from the microtubule (E3413, R3444, E3460, and C3469). These suggest that nucleotide-sensitive affinity may be locally controlled at the site of contact. Our work is the first detailed description of dynein-tubulin interactions and provides a framework for understanding how affinity is achieved and modulated.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.