EMDB-4169: N terminal region of dynein tail domains in complex with dynactin...

Basic information

• Entry: Database: EMDB / ID: EMD-4169
• Title: N terminal region of dynein tail domains in complex with dynactin filament and BICDR-1
• Map data: Map of the N-terminal half of two dynein tail domains bound to dynactin and BICDR1. This map was generated after particle signal subtraction from the overall map (separate deposition)

Sample

• Complex: Two dynein tail domains bound to dynactin and BICDR1.
  • Complex: dynactin filament
    • Protein or peptide: ARP1 actin related protein 1 homolog A
    • Protein or peptide: Capping protein (Actin filament) muscle Z-line, alpha 1
    • Protein or peptide: F-actin capping protein beta subunit
    • Protein or peptide: Dynactin subunit 2
    • Protein or peptide: Dynactin subunit 2
  • Complex: Cytoplasmic dynein
    • Protein or peptide: Cytoplasmic dynein 1 heavy chain 1
    • Protein or peptide: Cytoplasmic dynein 1 intermediate chain 2
  • Complex: BICDR1
    • Protein or peptide: BICD family-like cargo adapter 1
• Ligand: ADENOSINE-5'-DIPHOSPHATE

Function / homology

Function:

RHOD GTPase cycle / Factors involved in megakaryocyte development and platelet production / Golgi to secretory granule transport / RHOF GTPase cycle / dynactin complex / Regulation of PLK1 Activity at G2/M Transition / Loss of Nlp from mitotic centrosomes / Recruitment of mitotic centrosome proteins and complexes / Loss of proteins required for interphase microtubule organization from the centrosome / Anchoring of the basal body to the plasma membrane / AURKA Activation by TPX2 / transport along microtubule / WASH complex / F-actin capping protein complex / positive regulation of intracellular transport / dynein light chain binding / negative regulation of filopodium assembly / regulation of metaphase plate congression / dynein heavy chain binding / establishment of spindle localization / axonemal dynein complex / positive regulation of spindle assembly / vesicle transport along microtubule / dynein complex / COPI-independent Golgi-to-ER retrograde traffic / P-body assembly / minus-end-directed microtubule motor activity / barbed-end actin filament capping / dynein light intermediate chain binding / cytoplasmic dynein complex / regulation of cell morphogenesis / retrograde axonal transport / regulation of lamellipodium assembly / nuclear migration / Recruitment of NuMA to mitotic centrosomes / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MHC class II antigen presentation / COPI-mediated anterograde transport / microtubule motor activity / dynein intermediate chain binding / microtubule-based movement / cytoplasmic microtubule / dynactin binding / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / COPI-mediated anterograde transport / stress granule assembly / Mitotic Prometaphase / cytoplasmic microtubule organization / EML4 and NUDC in mitotic spindle formation / regulation of mitotic spindle organization / Loss of Nlp from mitotic centrosomes / Loss of proteins required for interphase microtubule organization from the centrosome / axon cytoplasm / Recruitment of mitotic centrosome proteins and complexes / cytoskeleton organization / Recruitment of NuMA to mitotic centrosomes / Resolution of Sister Chromatid Cohesion / Anchoring of the basal body to the plasma membrane / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / MHC class II antigen presentation / sarcomere / AURKA Activation by TPX2 / mitotic spindle organization / filopodium / RHO GTPases Activate Formins / cell morphogenesis / small GTPase binding / Aggrephagy / HCMV Early Events / Separation of Sister Chromatids / neuron projection development / Regulation of PLK1 Activity at G2/M Transition / azurophil granule lumen / actin filament binding / positive regulation of cold-induced thermogenesis / actin binding / cell cortex / actin cytoskeleton organization / microtubule / vesicle / cell division / centrosome / Neutrophil degranulation / ATP hydrolysis activity / RNA binding / extracellular exosome / extracellular region / ATP binding / membrane / cytoplasm / cytosol

Domain/homology:

Dynamitin / Dynamitin / Cytoplasmic dynein 1 intermediate chain 1/2 / Cytoplasmic dynein 1 intermediate chain 2 / F-actin-capping protein subunit beta / F-actin capping protein, beta subunit, conserved site / F-actin-capping protein subunit beta, N-terminal domain / F-actin capping protein, beta subunit / F-actin capping protein beta subunit signature. / F-actin capping protein, alpha subunit, conserved site / F-actin capping protein alpha subunit signature 1. / F-actin capping protein alpha subunit signature 2. / F-actin-capping protein subunit alpha / F-actin-capping protein subunit alpha/beta / F-actin-capping protein subunit alpha/beta, domain 2 / F-actin capping protein, alpha subunit, domain 1 / F-actin capping protein alpha subunit / Dynein heavy chain, AAA 5 extension domain / Dynein heavy chain AAA lid domain / Dynein heavy chain, C-terminal domain / Dynein heavy chain, C-terminal domain, barrel region / Dynein heavy chain C-terminal domain / P-loop containing dynein motor region / Dynein heavy chain, tail / Dynein heavy chain, N-terminal region 1 / Dynein heavy chain / Dynein heavy chain region D6 P-loop domain / Dynein heavy chain, linker / Dynein heavy chain, AAA module D4 / Dynein heavy chain, coiled coil stalk / Dynein heavy chain, hydrolytic ATP-binding dynein motor region / Dynein heavy chain, ATP-binding dynein motor region / Dynein heavy chain AAA lid domain / Dynein heavy chain AAA lid domain superfamily / Dynein heavy chain, domain 2, N-terminal / Dynein heavy chain, linker, subdomain 3 / Dynein heavy chain, AAA1 domain, small subdomain / Dynein heavy chain region D6 P-loop domain / Dynein heavy chain, N-terminal region 2 / Hydrolytic ATP binding site of dynein motor region / Microtubule-binding stalk of dynein motor / P-loop containing dynein motor region D4 / ATP-binding dynein motor region / Dynein heavy chain AAA lid domain / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / ATPase, nucleotide binding domain / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase

Component:

BICD family-like cargo adapter 1 / F-actin-capping protein subunit alpha-1 / F-actin-capping protein subunit beta / Dynactin subunit 2 / Dynactin subunit 2 / Alpha-centractin / Cytoplasmic dynein 1 intermediate chain 2 / Cytoplasmic dynein 1 heavy chain 1

• Biological species: Sus scrofa (pig) / Homo sapiens (human) / Mus musculus (house mouse) / Pig (pig)
• Method: single particle reconstruction / cryo EM / Resolution: 3.4 Å
• Authors: Urnavicius L / Lau CK / Elshenawy MM / Morales-Rios E / Motz C / Yildiz A / Carter AP

Funding support

United Kingdom, 2 items

Organization	Grant number	Country
Medical Research Council (United Kingdom)	MC_UP_A025_1011	United Kingdom
Wellcome Trust	WT100387	United Kingdom

• Citation: Journal: Nature / Year: 2018; Title: Cryo-EM shows how dynactin recruits two dyneins for faster movement.; Authors: Linas Urnavicius / Clinton K Lau / Mohamed M Elshenawy / Edgar Morales-Rios / Carina Motz / Ahmet Yildiz / Andrew P Carter / ; Abstract: Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. Here we use electron microscopy and single-molecule studies to show that adaptors can recruit a second dynein to dynactin. Whereas BICD2 is biased towards recruiting a single dynein, the adaptors BICDR1 and HOOK3 predominantly recruit two dyneins. We find that the shift towards a double dynein complex increases both the force and speed of the microtubule motor. Our 3.5 Å resolution cryo-electron microscopy reconstruction of a dynein tail-dynactin-BICDR1 complex reveals how dynactin can act as a scaffold to coordinate two dyneins side-by-side. Our work provides a structural basis for understanding how diverse adaptors recruit different numbers of dyneins and regulate the motile properties of the dynein-dynactin transport machine.

History

Deposition	Nov 23, 2017	-
Header (metadata) release	Jan 17, 2018	-
Map release	Jan 17, 2018	-
Update	Dec 11, 2019	-
Current status	Dec 11, 2019	Processing site: PDBe / Status: Released