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Cited by 421Microtubule and mitosis dynamicsGenetic and Kidney Cyst DiseasesProtein Structure and Dynamics

The structure of the dynactin complex and its interaction with dynein

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Urnavicius, Linas, Zhang, Kai, Diamant, Aristides G., Motz, Carina, Schlager, Max A., Yu, Minmin, Patel, Nisha A., Robinson, Carol V. +1 more·2015·Science
DOI 10.1126/science.aaa4080PMC PMC4413427
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Abstract

Making a molecular motor fit for purpose: Dynactin is an essential cofactor of the microtubule motor, cytoplasmic dynein. Dynactin contains 23 subunits built around a short filament of an actin-related protein (Arp1). How dynactin is assembled, how it functions with dynein, and why it is built around an actin-like filament is unclear. Urnavicius et al. combined cryo–electron microscopy structural studies and a crystal structure to determine the three-dimensional architecture of dynactin and how it interacts with dynein. Science , this issue p. 1441

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  • In the PDB dataset, a dimeric CC in a cryo-EM structure of the motor-protein dynein tail-dynactin-BICD2N complex (PDB ID 5afu) has a helix spanning 165 residues.

    “For instance, in the PDB dataset, a dimeric CC in a cryo‐EM structure of the motor‐protein dynein tail‐dynactin‐BICD2N complex (PDB ID, 5afu) (Urnavicius et al., 2015) has a helix spanning 165 residues.”

    From <scp> CC <sup>+</sup> </scp> : A searchable database of validated coiled coils in <scp>PDB</scp> structures and <scp>AlphaFold2</scp> models (2023) · cites this paper as Urnavicius et al., 2015

    In “Dynein and BICD bind the dynactin filament” (page unavailable), the paper reports an 8.2 Å cryo-EM structure of the dynein tail–dynactin–BICD2N complex and a BICD2N coiled coil. Our copy does not identify that structure as PDB 5afu or state that a helix spans 165 residues; it describes the coiled coil as approximately 270 residues long. (LLM, conf=0.85)

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Cites

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Authors
Urnavicius, L., Zhang, K., Diamant, A. G., Motz, C., Schlager, M. A., Yu, M., Patel, N. A., Robinson, C. V., & Carter, A. P.
Affiliations
  • MRC Laboratory of Molecular Biology (GB)
  • University of Oxford (GB)
Corresponding author
  • Urnavicius, Linas
  • Zhang, Kai
  • Diamant, Aristides G.
  • Carter, Andrew P.
ORCID
Venue
Science
Publisher
American Association for the Advancement of Science (AAAS)
Published
2015-03-27
Volume
347
Issue
6229
Pages
1441-1446
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
DOI
10.1126/science.aaa4080
PMC
PMC4413427
OpenAlex
W2061126550
Cited by
421
References
1
Citations by year
2026: 24 · 2025: 36 · 2024: 25 · 2023: 39 · 2022: 36 · 2021: 39 · 2020: 40 · 2019: 35 · 2018: 52 · 2017: 48 · 2016: 30 · 2015: 17
FWCI
26.30
Type
journal article
Language
en
Open access
Licence
www.sciencemag.org/about/science-licenses-journal-article-reuse (vor, 366 d)
Locations
  • Science (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • Wellcome Trust (WT100387)
  • Medical Research Council, UK (MC_UP_A025_1011)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
dynactin, cytoplasmic dynein-1, Arp1, beta-actin, microtubule motor proteins, cryo-EM structure, coiled coil, cargo adaptors
MeSH terms
Dynactin Complex, Actins, Animals, Dyneins, Humans, Microtubule-Associated Proteins, Swine, Protein Structure, Secondary, Protein Structure, Tertiary, Cryoelectron Microscopy, Protein Subunits, Protein Interaction Mapping, Multiprotein Complexes, Mice

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