NUDEL Is a Novel Cdk5 Substrate that Associates with LIS1 and Cytoplasmic Dynein

@article{Niethammer2000NUDELIA,
  title={NUDEL Is a Novel Cdk5 Substrate that Associates with LIS1 and Cytoplasmic Dynein},
  author={Martin Niethammer and Deanna S. Smith and Rams{\'e}s Ayala and Junmin Peng and Jane Ko and Ming sum Lee and Maria A. Morabito and Li-Huei Tsai},
  journal={Neuron},
  year={2000},
  volume={28},
  pages={697-711}
}
Disruption of one allele of the LIS1 gene causes a severe developmental brain abnormality, type I lissencephaly. In Aspergillus nidulans, the LIS1 homolog, NUDF, and cytoplasmic dynein are genetically linked and regulate nuclear movements during hyphal growth. Recently, we demonstrated that mammalian LIS1 regulates dynein functions. Here we characterize NUDEL, a novel LIS1-interacting protein with sequence homology to gene products also implicated in nuclear distribution in fungi. Like LIS1… 
A LIS1/NUDEL/Cytoplasmic Dynein Heavy Chain Complex in the Developing and Adult Nervous System
TLDR
It is demonstrated that LIS1 directly interacts with the cytoplasmic dynein heavy chain (CDHC) and NUDEL, a murine homolog of the Aspergillus nidulans nuclear migration mutant NudE, and establishes a direct functional link between LIS2, NudEL, and microtubule motors.
LIS1 Regulates CNS Lamination by Interacting with mNudE, a Central Component of the Centrosome
TLDR
LIS1 interacting protein encoded by a mouse homolog of NUDE, a nuclear distribution gene in A. nidulans and a multicopy suppressor of the LIS1 homolog, NUDF are identified, which may regulate neuronal migration through dynamic reorganization of the MTOC.
Human Nudel and NudE as Regulators of Cytoplasmic Dynein in Poleward Protein Transport along the Mitotic Spindle
TLDR
It is demonstrated that a Nudel mutant incapable of binding to Lis1 impaired the poleward movement of dynein and hence the dyneIn-mediated transport of kinetochore proteins to spindle poles along microtubules, a process contributing to inactivation of the spindle checkpoint in mitosis.
LIS1 and NudE Induce a Persistent Dynein Force-Producing State
TLDR
It is found that NudE stably recruits LIS1 to the dynein holoenzyme molecule, where LIS2 interacts with the motor domain during the prepowerstroke state of the dyNEin crossbridge cycle, which likely explains the requirement for L IS1 and NUDE in the transport of nuclei, centrosomes, chromosomes, and the microtubule cytoskeleton.
The essential role of LIS1, NDEL1 and Aurora-A in polarity formation and microtubule organization during neurogensis
TLDR
Physiological functions of LIS1 and NDEL1 in neurons have been ascribed for proteins fundamentally required for cell cycle progression and control and may exert other functions during neurogenesis in a direct or an indirect fashion.
A Cdk5-Dependent Switch Regulates Lis1/Ndel1/Dynein-Driven Organelle Transport in Adult Axons
TLDR
The data raise the possibility that defects in a Lis1/Ndel1 regulatory switch could contribute to neurodegenerative diseases linked to axonal pathology in adults.
Nudel functions in membrane traffic mainly through association with Lis1 and cytoplasmic dynein
TLDR
It is concluded that Nudel is critical for Dynein motor activity in membrane transport and possibly other cellular activities through interactions with both Lis1 and dynein heavy chain.
Ndel1 Operates in a Common Pathway with LIS1 and Cytoplasmic Dynein to Regulate Cortical Neuronal Positioning
TLDR
RNAi results provide strong evidence that Ndel1 interacts with LIS1 to sustain the function of dynein, which in turn impacts microtubule organization, nuclear translocation, and neuronal positioning.
LIS1 Let's Interact Sometimes… (Part 1)
TLDR
Together, these results suggest a migration that result in poor organization of the cortical similarity of mechanism between nuclear movement in layering and a reduced surface area and lack of cortical fungi and neuronal migration.
Cytoplasmic LEK1 is a regulator of microtubule function through its interaction with the LIS1 pathway.
TLDR
Data is presented that cytoplasmic LEK1 (cytLEK1), a large protein containing a spectrin repeat and multiple leucine zippers, is a component of this pathway through its direct interaction with NudE, as determined by a yeast two-hybrid screen.
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References

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A LIS1/NUDEL/Cytoplasmic Dynein Heavy Chain Complex in the Developing and Adult Nervous System
TLDR
It is demonstrated that LIS1 directly interacts with the cytoplasmic dynein heavy chain (CDHC) and NUDEL, a murine homolog of the Aspergillus nidulans nuclear migration mutant NudE, and establishes a direct functional link between LIS2, NudEL, and microtubule motors.
LIS1 Regulates CNS Lamination by Interacting with mNudE, a Central Component of the Centrosome
TLDR
LIS1 interacting protein encoded by a mouse homolog of NUDE, a nuclear distribution gene in A. nidulans and a multicopy suppressor of the LIS1 homolog, NUDF are identified, which may regulate neuronal migration through dynamic reorganization of the MTOC.
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TLDR
The cloning of the nudA gene by complementation of the mutant phenotype by using a chromosome VIII-specific cosmid library is described and in vivo evidence that dynein, a microtubule motor molecule, plays a role in the nuclear migration process is provided.
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TLDR
The results indicate that abundance of Lis1 in neurons may stimulate specific dynein functions that function in neuronal migration and axon growth.
NudF, a nuclear migration gene in Aspergillus nidulans, is similar to the human LIS-1 gene required for neuronal migration.
TLDR
A gene, nudF, which is required for nuclear migration during vegetative growth as well as development is cloned, suggesting that the LIS-1 gene product may have a function similar to that of NUDF and supports previous findings to suggest that nuclear migration may play a role in neuronal migration.
The Lis1-Related Nudf Protein of Aspergillus nidulans Interacts with the Coiled-Coil Domain of the Nude/Ro11 Protein
TLDR
NUDF protein, the product of the nudF gene, displays 42% sequence identity with the human protein LIS1 required for neuronal migration, which strengthens the notion that these two proteins are functionally related.
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TLDR
It is shown that Drosophila Lis1 is highly expressed in the nervous system and is essential for neuroblast proliferation and axonal transport, as shown by a mosaic analysis using a Lis1 null mutation.
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TLDR
It is suggested that LIS1 activity may be regulated by phosphorylation, one of the ways to control cellular localization and protein-protein interactions, as well as CAK-inducing activity.
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TLDR
It is found that p25, a truncated form of p35, accumulates in neurons in the brains of patients with Alzheimer's disease, and this accumulation correlates with an increase in Cdk5 kinase activity.
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