Mechanism and regulation of cytoplasmic dynein.

No abstract is available for this paper.

• Publication year

  2015

• Venue

  Annual Review of Cell and Developmental Biology

• Publication date

  2015-11-13

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1146/annurev-cellbio-100814-125438PMID 26436706PMCID PMC4644480
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• Cytoplasmic dynein is required for the spatial organization of protein aggregates in filamentous fungi.

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• The structure of the dynactin complex and its interaction with dynein

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• Cytoplasmic dynein regulates its attachment to microtubules via nucleotide state-switched mechanosensing at multiple AAA domains

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• Regulation of processive motion and microtubule localization of cytoplasmic dynein.

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• Integrated regulation of motor-driven organelle transport by scaffolding proteins.

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• In vitro reconstitution of a highly processive recombinant human dynein complex

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• Autoinhibition and cooperative activation mechanisms of cytoplasmic dynein

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• Activation of cytoplasmic dynein motility by dynactin-cargo adapter complexes

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• Autoregulatory Mechanism for Dynactin Control of Processive and Diffusive Dynein Transport

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• Axonal transport: cargo-specific mechanisms of motility and regulation.

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• THE AAA3 DOMAIN OF CYTOPLASMIC DYNEIN ACTS AS A SWITCH TO FACILITATE MICROTUBULE RELEASE

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• Reconstitution of dynein transport to the microtubule plus end by kinesin

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• Dynactin 3D structure: implications for assembly and dynein binding.

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• HookA is a novel dynein–early endosome linker critical for cargo movement in vivo

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• Lis1 regulates dynein by sterically blocking its mechanochemical cycle

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• LIS1 controls mitosis and mitotic spindle organization via the LIS1-NDEL1-dynein complex.

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• Reconstitution of a hierarchical +TIP interaction network controlling microtubule end tracking of dynein

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• Mutations in cytoplasmic dynein and its regulators cause malformations of cortical development and neurodegenerative diseases.

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• Axonal transport deficits and neurodegenerative diseases

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• Mutations in TUBG1, DYNC1H1, KIF5C and KIF2A cause malformations of cortical development and microcephaly

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• LIS1 functions in normal development and disease.

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• Molecular defects in the motor adaptor BICD2 cause proximal spinal muscular atrophy with autosomal-dominant inheritance.

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• Microtubule-dependent endosomal sorting of clathrin-independent cargo by Hook1

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• Lissencephaly-1 promotes the recruitment of dynein and dynactin to transported mRNAs

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• Mutations in BICD2 cause dominant congenital spinal muscular atrophy and hereditary spastic paraplegia.

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• Mutations in BICD2, which encodes a golgin and important motor adaptor, cause congenital autosomal-dominant spinal muscular atrophy.

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• Distinct Functions of Nuclear Distribution Proteins LIS1, Ndel1 and NudCL in Regulating Axonal Mitochondrial Transport

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• Bicaudal-D uses a parallel, homodimeric coiled coil with heterotypic registry to coordinate recruitment of cargos to dynein.

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• Dynactin Subunit p150Glued Is a Neuron-Specific Anti-Catastrophe Factor

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• Ordered Recruitment of Dynactin to the Microtubule Plus-End is Required for Efficient Initiation of Retrograde Axonal Transport

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• Intrinsic Disorder in Dynein Intermediate Chain Modulates Its Interactions with NudE and Dynactin*

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• BICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment to cellular structures

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• Cytoplasmic Dynein Moves Through Uncoordinated Stepping of the AAA+ Ring Domains

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• Autophagosomes initiate distally and mature during transport toward the cell soma in primary neurons

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• LIS1 Duplication

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• The 2.8 Å crystal structure of the dynein motor domain

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• Dynactin is required for transport initiation from the distal axon.

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• Insights into dynein motor domain function from a 3.3 Å crystal structure

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• Dynactin's pointed-end complex is a cargo-targeting module

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• Lis1 is an initiation factor for dynein-driven organelle transport

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• Mutations in the tail domain of DYNC1H1 cause dominant spinal muscular atrophy

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• The p150(Glued) CAP-Gly domain regulates initiation of retrograde transport at synaptic termini.

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• Lis1 Acts as a “Clutch” between the ATPase and Microtubule-Binding Domains of the Dynein Motor

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• Structural Basis for Microtubule Binding and Release by Dynein

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• Dynein achieves processive motion using both stochastic and coordinated stepping

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• Coupling viruses to dynein and kinesin‐1

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• Cytoplasmic dynein.

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