Mouse Cytoplasmic Dynein Intermediate Chains: Identification of New Isoforms, Alternative Splicing and Tissue Distribution of Transcripts

@article{Kuta2010MouseCD,
  title={Mouse Cytoplasmic Dynein Intermediate Chains: Identification of New Isoforms, Alternative Splicing and Tissue Distribution of Transcripts},
  author={Anna Kuta and Wenhan Deng and Ali S Morsi El-Kadi and Gareth T. Banks and Majid Hafezparast and Katherine Pfister and Elizabeth M. C. Fisher},
  journal={PLoS ONE},
  year={2010},
  volume={5}
}
Background Intracellular transport of cargoes including organelles, vesicles, signalling molecules, protein complexes, and RNAs, is essential for normal function of eukaryotic cells. The cytoplasmic dynein complex is an important motor that moves cargos along microtubule tracks within the cell. In mammals this multiprotein complex includes dynein intermediate chains 1 and 2 which are encoded by two genes, Dync1i1 and Dync1i2. These proteins are involved in dynein cargo binding and dynein… Expand
Distinct functional roles of cytoplasmic dynein defined by the intermediate chain isoforms.
  • K. Pfister
  • Biology, Medicine
  • Experimental cell research
  • 2015
TLDR
Data support the model that cytoplasmic dynein can be specifically regulated through the different isoforms of the subunits, as well as the role the intermediate chains play a key scaffold role in the dyneIn complex. Expand
Investigation of subunits of the cytoplasmic dynein complex using novel mouse models
TLDR
To examine the effects of mutation at the cellular level primary mouse embryonic fibroblasts lines were derived from embryos carrying mutations in the intermediate chains and used as a model system and biochemical analyses were performed focused on the expression of dynein subunits and their assembly in the functional complex. Expand
Cytoplasmic dynein function defined by subunit composition
TLDR
The study illustrates that distinct Dynein functions are correlated with dynein complexes containing different isoforms of the intermediate chain (IC), the light-intermediate chain (LIC), or the DYNLT LC, and suggests that the LIC and DYN LT isoforms are specific for different cellular “housekeeping” dyne in functions. Expand
Behavioral and Other Phenotypes in a Cytoplasmic Dynein Light Intermediate Chain 1 Mutant Mouse
TLDR
It is found that an N235Y point mutation in this protein results in altered neuronal development, as shown from in vivo studies in the developing cortex, and analyses of electrophysiological function, thus linking dynein functions to a behavioral phenotype in mammals for the first time. Expand
Trk Activation of the ERK1/2 Kinase Pathway Stimulates Intermediate Chain Phosphorylation and Recruits Cytoplasmic Dynein to Signaling Endosomes for Retrograde Axonal Transport
TLDR
Results demonstrate that neurotrophin binding to Trk initiates the recruitment of cytoplasmic dynein to signaling endosomes through ERK1/2 phosphorylation of intermediate chains for their subsequent retrograde transport in axons. Expand
The interplay between dynein, accessory proteins and the endocytic pathway
TLDR
The results from this project show that dynactin recruitment to intracellular membranes, including RILP-postivie membranes, requires dynein, and Lis1 and LIC1 or LIC2 are necessary but not sufficient, individually, to recruit dyne in and dynact in to RilP-positive membranes. Expand
Establishing a novel knock‐in mouse line for studying neuronal cytoplasmic dynein under normal and pathologic conditions
TLDR
A novel knock‐in mouse line is established in which the neuron‐specific cytoplasmic dynein 1 intermediate chain 1 (IC‐1) is tagged with both GFP and a 3xFLAG tag at its C‐terminus, and the IC‐1‐GFP‐3xFLAG fusion protein is incorporated into the endogenous dyne in complex. Expand
Neurodegenerative Mutation in Cytoplasmic Dynein Alters Its Organization and Dynein-Dynactin and Dynein-Kinesin Interactions*
TLDR
It is found that the Loa mutation in the heavy chain leads to increased affinity of this subunit of cytoplasmic dynein to light intermediate and a population of intermediate chains and a suppressed association of dynactin to Dynein. Expand
In vitro reconstitution of a highly processive recombinant human dynein complex
TLDR
The production of a fully recombinant human dynein complex from a single baculovirus in insect cells and single‐molecule fluorescence microscopy provides insight into a novel mechanism for coordinating cargo binding with long‐distance motor movement. Expand
Live cell imaging of cytoplasmic dynein movement in transfected embryonic rat neurons.
TLDR
A method to study its location and motility in living cells using the long thin axons of cultured hippocampal neurons and fluorescent subunit probes, which can be used to identify specific cargos of dynein complexes with different IC isoforms as well as the kinetic properties of cytoplasmic Dynein. Expand
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References

SHOWING 1-10 OF 48 REFERENCES
Cytoplasmic Dynein Intermediate-Chain Isoforms with Different Targeting Properties Created by Tissue-Specific Alternative Splicing
TLDR
Evidence is presented that in Drosophila, the IC subunits are represented by at least 10 structural isoforms, created by the alternative splicing of transcripts from a unique Cdic gene, and a mechanism is proposed for the regulation of dynein binding to organelles through the changes in the content of the IC isoform pool. Expand
Intermediate chain subunit as a probe for cytoplasmic dynein function: Biochemical analyses and live cell imaging in PC12 cells
TLDR
Protein binding studies showed that all six intermediate chains were able to bind to the mutated heavy chain and live cell imaging and comparative immunocytochemical analyses show that dynein is enriched in the actin rich region of growth cones. Expand
Identification and developmental regulation of a neuron-specific subunit of cytoplasmic dynein.
TLDR
It is found that between the fifteenth day of gestation (E15) and the fifth day after birth (P5), the relative expression of the IC74 protein isoforms changes, demonstrating that the expression of IC74 isoforms is developmentally regulated in brain. Expand
Growth factor regulation of cytoplasmic dynein intermediate chain subunit expression preceding neurite extension
TLDR
The growth factor induced changes in the expression of dynein intermediate chains suggests that specific intermediate chain isoforms are utilized during axon growth. Expand
Identification of a Novel Region of the Cytoplasmic Dynein Intermediate Chain Important for Dimerization in the Absence of the Light Chains*
TLDR
Co-immunoprecipitation analyses were used to demonstrate that all combinations of homo- and heterodimers of the six intermediate chains are possible and the formation of dynein complexes with different combinations of isoforms is not limited by interaction between the various intermediate chains. Expand
Differential Expression and Phosphorylation of the 74-kDa Intermediate Chains of Cytoplasmic Dynein in Cultured Neurons and Glia (*)
TLDR
It is found that cultured cortical neurons and glia express distinct IC74 isoforms, and a single mRNA product and its phosphoisoform are sufficient for constitutive dynein function and regulation in glial cells. Expand
Interaction of the DYNLT (TCTEX1/RP3) Light Chains and the Intermediate Chains Reveals Novel Intersubunit Regulation during Assembly of the Dynein Complex*
TLDR
Yeast two-hybrid and co-immunoprecipitation assays demonstrate that both members of the DYNLT family are capable of forming homodimer and heterodimers, and not all of the possible combinations of the isoforms are utilized during the assembly of the dynein complex. Expand
Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued
TLDR
Findings identify a direct interaction between two specific component polypeptides and support a role for dynactin as a dynein "receptor" and suggest, however, that this interaction must be highly regulated. Expand
Cloning and characterization of two cytoplasmic dynein intermediate chain genes in mouse and human.
TLDR
The identification of the human homologue of cytoplasmic dynein intermediate chain 1 gene (DNCI1) located on human chromosome 7q21.3-q22.1 provides a framework for the further analysis of the functional role of Dnci1 and DnCI2 in mouse and DNCI1 in human. Expand
Structural and thermodynamic characterization of a cytoplasmic dynein light chain–intermediate chain complex
TLDR
The structure and thermodynamic analysis of a complex of LC8 and TcTex1 associated with their intermediate chain scaffold suggest that, in the dynein complex, the LCs do not bind cargo, in apparent disagreement with a role for LCs in dyne in cargo binding interactions. Expand
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