ArticleMolecular biology of the cell1997
The involvement of the intermediate chain of cytoplasmic dynein in binding the motor complex to membranous organelles of Xenopus oocytes.
Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 108 citations in OpenAlex.
- CDR2 is a dynein adaptor recruited by kinectin to regulate ER sheet organization.The Journal of cell biology · 2025Article
- Dynein-dependent collection of membranes defines the architecture and position of microtubule asters in isolated, geometrically confined volumes of cell-free extracts.Molecular biology of the cell · 2022Article
- Optimizing Efficiency and Motility of a Polyvalent Molecular Motor.Micromachines · 2022Article
- A novel, dynein-independent mechanism focuses the endoplasmic reticulum around spindle poles in dividing Drosophila spermatocytes.Scientific reports · 2019Article
- Inositol hexakisphosphate kinase 3 promotes focal adhesion turnover via interactions with dynein intermediate chain 2.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The cytoplasmic dynein transport machinery and its many cargoes.Nature reviews. Molecular cell biology · 2018Review
- Microtubule assembly crucial to bovine embryonic development in assisted reproductive technologies.Animal science journal = Nihon chikusan Gakkaiho · 2016Review
- Multiple mechanisms determine ER network morphology during the cell cycle in Xenopus egg extracts.The Journal of cell biology · 2013Article
- Lissencephaly-1 promotes the recruitment of dynein and dynactin to transported mRNAs.The Journal of cell biology · 2013Article
- Trk activation of the ERK1/2 kinase pathway stimulates intermediate chain phosphorylation and recruits cytoplasmic dynein to signaling endosomes for retrograde axonal transport.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Analyses of dynein heavy chain mutations reveal complex interactions between dynein motor domains and cellular dynein functions.Genetics · 2012Article
- Misfolded Gβ is recruited to cytoplasmic dynein by Nudel for efficient clearance.Cell research · 2012Article
- Evolution of the eukaryotic dynactin complex, the activator of cytoplasmic dynein.BMC evolutionary biology · 2012Article
- The axonal transport of mitochondria.Journal of cell science · 2012Review
- Mutually exclusive cytoplasmic dynein regulation by NudE-Lis1 and dynactin.The Journal of biological chemistry · 2011Article
- Dynein light intermediate chain: an essential subunit that contributes to spindle checkpoint inactivation.Molecular biology of the cell · 2008Article
- Cytoplasmic dynein and LIS1 are required for microtubule advance during growth cone remodeling and fast axonal outgrowth.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007Article
- The kinesin KIF1C and microtubule plus ends regulate podosome dynamics in macrophages.Molecular biology of the cell · 2006Article
- Genetic analysis of the cytoplasmic dynein subunit families.PLoS genetics · 2006Article
- Three-dimensional reconstruction of the dynactin complex by single-particle image analysis.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 3 countries.
Funding
Abstract
Cytoplasmic dynein is one of the major motor proteins involved in intracellular transport. It is a protein complex consisting of four subunit classes: heavy chains, intermediate chains (ICs), light intermediate chains, and light chains. In a previous study, we had generated new monoclonal antibodies to the ICs and mapped the ICs to the base of the motor. Because the ICs have been implicated in targeting the motor to cargo, we tested whether these new antibodies to the intermediate chain could block the function of cytoplasmic dynein. When cytoplasmic extracts of Xenopus oocytes were incubated with either one of the monoclonal antibodies (m74-1, m74-2), neither organelle movement nor network formation was observed. Network formation and membrane transport was blocked at an antibody concentration as low as 15 micrograms/ml. In contrast to these observations, no effect was observed on organelle movement and tubular network formation in the presence of a control antibody at concentrations as high as 0.5 mg/ml. After incubating cytoplasmic extracts or isolated membranes with the monoclonal antibodies m74-1 and m74-2, the dynein IC polypeptide was no longer detectable in the membrane fraction by SDS-PAGE immunoblot, indicating a loss of cytoplasmic dynein from the membrane. We used a panel of dynein IC truncation mutants and mapped the epitopes of both antibodies to the N-terminal coiled-coil domain, in close proximity to the p150Glued binding domain. In an IC affinity column binding assay, both antibodies inhibited the IC-p150Glued interaction. Thus these findings demonstrate that direct IC-p150Glued interaction is required for the proper attachment of cytoplasmic dynein to membranes.
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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.