| 2000 |
NUDEL (NDEL1) was identified as a novel LIS1-interacting protein and a substrate of Cdk5 kinase. NUDEL is enriched at centrosomes and neuronal growth cones and interacts with cytoplasmic dynein. Inhibition of Cdk5 modifies NUDEL distribution in neurons and affects neuritic morphology. |
Co-immunoprecipitation, subcellular fractionation, in vitro kinase assay, immunofluorescence |
Neuron |
High |
11163260
|
| 2003 |
14-3-3epsilon binds to CDK5/p35-phosphorylated NUDEL and this binding maintains NUDEL phosphorylation. Deficiency of 14-3-3epsilon results in mislocalization of NUDEL and LIS1, consistent with reduction of cytoplasmic dynein function. |
Co-immunoprecipitation, genetic mouse models (Ywhae knockout/heterozygous), immunolocalization |
Nature genetics |
High |
12796778
|
| 2002 |
DISC1 interacts with NUDEL (NDEL1) via yeast two-hybrid, and the disease-associated truncation mutant of DISC1 fails to bind NUDEL. Expression of mutant DISC1 in PC12 cells reduces neurite extension. |
Yeast two-hybrid, co-immunoprecipitation, neurite outgrowth assay in PC12 cells |
Proceedings of the National Academy of Sciences of the United States of America |
High |
12506198
|
| 2003 |
DISC1 interacts with NUDEL through a central coiled-coil domain of DISC1 that binds the C-terminal domain of NUDEL, independent from the LIS1 binding site on NUDEL. NUDEL acts as a bridge between DISC1 and LIS1, allowing formation of a trimolecular complex. |
Yeast two-hybrid, mammalian two-hybrid, co-immunoprecipitation, deletion mapping |
Human molecular genetics |
High |
12812986 14962739
|
| 2004 |
Ndel1 positively regulates dynein activity by facilitating the interaction between LIS1 and dynein. Loss of Ndel1 in developing neocortex impairs neuronal positioning and causes uncoupling of the centrosome and nucleus. Overexpression of LIS1 partially rescues the positioning defect caused by Ndel1 RNAi, placing Ndel1 upstream of dynein and in common pathway with LIS1. |
RNA interference in developing neocortex (in utero), epistasis rescue experiments, immunofluorescence |
Neuron |
High |
15473966
|
| 2003 |
Nudel (NDEL1) is specifically phosphorylated in M phase by Cdc2 (CDK1) and by Erk1/2. Phosphorylation regulates its cell-cycle-dependent distribution and increases its association with Lis1. A Nudel mutant incapable of binding Lis1 impaired poleward movement of dynein and dynein-mediated transport of kinetochore proteins to spindle poles. |
In vitro kinase assays, phosphorylation-mimicking and phosphorylation-deficient mutants, immunofluorescence, functional mitosis assays |
Molecular and cellular biology |
High |
12556484
|
| 2005 |
Complete loss of Ndel1 results in embryonic lethality at the peri-implantation stage and cell proliferation defects. Compound heterozygous mice show neuronal migration defects. Ndel1 loss leads to abnormalities in microtubule organization and similar defects in dynein-dependent vesicle distribution as Lis1 loss. Rescue by LIS1, NDEL1, or NDE1 overexpression confirms they act in a common pathway. |
Targeted gene disruption (mouse knockout/hypomorph), MEF and granule cell assays, immunofluorescence, rescue experiments |
Molecular and cellular biology |
High |
16107726
|
| 2005 |
CDK5-mediated phosphorylation of NDEL1 facilitates interaction between NDEL1 and katanin p60, and phosphorylated NDEL1 regulates the distribution of katanin p60. Loss of NDEL1 causes abnormal accumulation of p60 in nucleus. Loss of NDEL1 or dominant negative p60 in migrating neurons causes defective migration and elongation of nuclear-centrosomal distance. |
Co-immunoprecipitation, phosphorylation assays, dominant-negative expression, neuronal migration assay |
Human molecular genetics |
High |
16203747
|
| 2006 |
Aurora-A phosphorylates NDEL1 at Ser251 at mitotic entry. This phosphorylation is required for centrosomal maturation and separation. NDEL1 is required for centrosome targeting of TACC3 through direct interaction with TACC3. Aurora-A phosphorylation-mimetic NDEL1 mutants rescue centrosomal maturation/separation defects in Aurora-A-depleted cells. |
In vitro kinase assay, phosphomimetic/phosphodeficient mutants, siRNA depletion rescue, immunofluorescence, co-immunoprecipitation |
Molecular and cellular biology |
High |
17060449
|
| 2007 |
DISC1 directly interacts with kinesin-1 heavy chain and links the NUDEL/LIS1/14-3-3epsilon complex to kinesin-1 for anterograde axonal transport. Knockdown of DISC1 inhibited accumulation of NUDEL, LIS1, and 14-3-3epsilon at axons and inhibited axon elongation. |
Co-immunoprecipitation, RNAi knockdown, immunofluorescence, axon elongation assay |
The Journal of neuroscience |
Medium |
17202468
|
| 2007 |
Cenp-F interacts with Ndel1 and Nde1, and Ndel1/Nde1/Lis1 localize to kinetochores in a Cenp-F-dependent manner. Inhibition of Ndel1 leads to chromosome malalignments not detected by the spindle checkpoint, resulting in lagging chromosomes during anaphase. Ndel1 and Nde1 play distinct roles at kinetochores. |
Co-immunoprecipitation, siRNA knockdown, live cell imaging, immunofluorescence |
Current biology |
High |
17600710
|
| 2007 |
Ndel1 is required for robust localization of dynein/dynactin at the kinetochore. Kinetochore localization of Nudel depends mostly (~78%) on mitosin (CENP-F) and slightly on dynein/dynactin. Nudel activates dynein-mediated protein transport at the kinetochore and stabilizes kinetochore dynein/dynactin against microtubule-dependent stripping. |
RNAi, mutant overexpression, time-lapse imaging, immunofluorescence |
Molecular biology of the cell |
Medium |
17494871
|
| 2007 |
Crystal structure of two fragments of the coiled-coil domain of Ndel1 (residues 10-166) revealed a stable parallel homodimer with supercoiled alpha helices. The structure suggests how the Lis1-interacting domain can be regulated via cooperative binding of two Ndel1 helices to a Lis1 homodimer. |
X-ray crystallography, solution studies (solution NMR/biophysics) |
Structure |
High |
17997972
|
| 2004 |
NUDEL directly interacts with neurofilament light subunit (NF-L) and facilitates the polymerization of neurofilaments. Knockdown of NUDEL by RNAi destabilizes NF-L and alters neurofilament homeostasis, resulting in morphological changes reminiscent of neurodegeneration. |
Co-immunoprecipitation, RNAi knockdown in neuroblastoma cells and primary cortical neurons, in vitro polymerization assay |
Nature cell biology |
High |
15208636
|
| 2004 |
Nudel (NDEL1) regulates dynein-mediated membrane transport through direct interactions with both Lis1 and dynein heavy chain. A Nudel mutant defective in Lis1 or dynein heavy chain binding causes dispersion of dynein-dependent membranous organelles and reduces frequency and velocity of lysosome minus-end-directed motions. |
Mutant overexpression, RNAi, time-lapse microscopy for lysosome motility, organelle localization assays |
The Journal of cell biology |
High |
14970193
|
| 2005 |
Nudel (Ndl1 in budding yeast) targets dynein to microtubule plus ends through LIS1. The Ndl1 null mutant shows decreased targeting of dynein to microtubule plus ends. Ndl1 regulates dynein targeting through LIS1 but not through CLIP170. |
Yeast genetics (null mutant), live cell imaging, biochemical interaction assays |
Nature cell biology |
High |
15965467
|
| 2005 |
Nudel (NDEL1) contributes to microtubule anchoring at the mother centriole. Nudel localizes to mother centriole and its centrosome localization requires a C-terminal region essential for associations with dynein, dynactin, PCM-1, pericentrin, and gamma-tubulin. Nudel plays roles in both dynein-mediated transport of dynactin/Lis1/PCM-1 and dynein-independent centrosomal targeting of pericentrin and gamma-tubulin. |
RNAi, mutant overexpression, immunofluorescence, co-immunoprecipitation |
Molecular biology of the cell |
Medium |
16291865
|
| 2008 |
LIS1 suppresses the motility of cytoplasmic dynein on microtubules, while NDEL1 releases the blocking effect of LIS1 on cytoplasmic dynein. LIS1 mediates anterograde transport of cytoplasmic dynein as a dynein-LIS1 complex on transportable microtubule fragments. |
In vitro microtubule motility assay, blocking antibody experiments, co-immunoprecipitation |
The EMBO journal |
High |
18784752
|
| 2008 |
Protein phosphatase 4 catalytic subunit (PP4c) dephosphorylates NDEL1 at CDK1 sites. Loss of PP4c leads to unscheduled CDK1 activation and abnormal NDEL1 phosphorylation, which causes excessive recruitment of katanin p60 to the centrosome and microtubule disorganization. Inhibition of CDK1, NDEL1, or katanin p60 rescues the defects caused by PP4 inhibition. |
In vitro phosphatase assay, targeted gene disruption, pharmacological CDK1 inhibition, epistasis rescue |
The Journal of cell biology |
High |
18347064
|
| 2008 |
Lis1 and Ndel1 reduction impairs prophase nuclear envelope invagination (PNEI), a dynein-dependent process facilitating nuclear envelope breakdown (NEBD). Ndel1 phosphorylation is important for this function, regulating binding to both Lis1 and dynein. |
siRNA knockdown, live cell imaging, phosphomimetic/phosphodeficient mutants, mouse brain histology |
The Journal of cell biology |
Medium |
18809722
|
| 2008 |
Nudel interacts with Cdc42GAP and competes with Cdc42 for binding Cdc42GAP, inhibiting Cdc42GAP-mediated inactivation of Cdc42 in a dose-dependent manner. Nudel's leading-edge localization in migrating cells requires phosphorylation by Erk1/2. Depleting Nudel or expressing a non-phosphorylatable mutant abolishes Cdc42 activation and cell migration. |
Co-immunoprecipitation, competitive binding assay, RNAi, phosphomimetic mutants, Cdc42 activation assay, migration assay |
Developmental cell |
High |
18331715
|
| 2008 |
Ndel1 forms a novel complex with vimentin, dynein, Lis1, and alphaCOP. Ndel1 promotes interaction between Lis1, alphaCOP, and the vimentin-dynein complex, activating dynein-mediated transport of vimentin. Loss of Ndel1 by RNAi fails to incorporate Lis1/alphaCOP in the complex, reduces vimentin transport, and alters neuritogenesis. |
Tandem affinity purification, co-immunoprecipitation, RNAi, transport assay |
The Journal of biological chemistry |
Medium |
18303022
|
| 2009 |
aPKC phosphorylates Aurora A at Thr287, which facilitates Aurora A interaction with TPX2 and activates Aurora A at the neurite hillock, leading to phosphorylation of NDEL1 at S251 and NDEL1 recruitment. Suppression of aPKC, Aurora A, TPX2, or Ndel1 impairs neurite extension. Suppression of this pathway decreases frequency of microtubule emanation from the MTOC. |
In vitro kinase assays, RNAi, phosphomimetic mutants, live microtubule plus-end marker imaging, immunofluorescence |
Nature cell biology |
High |
19668197
|
| 2009 |
Palmitoylation of Ndel1 by specific palmitoylation enzymes occurs in vivo. Unpalmitoylated Ndel1 interacts better with dynein; palmitoylated Ndel1 reduces cytoplasmic dynein activity, as shown by Golgi distribution, vesicle trafficking, retrograde transport of dynein, and neuronal migration assays. |
Palmitoylation assay (metabolic labeling), co-immunoprecipitation, organelle localization assays, neuronal migration assay, time-lapse imaging |
The EMBO journal |
High |
19927128
|
| 2009 |
Nudel binds to paxillin at nascent adhesions and colocalization is observed in areas of active membrane protrusions. Focal adhesion kinase (FAK) disrupts the Nudel-paxillin interaction in a paxillin-binding-dependent manner. Forced localization of Nudel to all focal contacts markedly strengthened adhesivity, while overexpression of activated FAK caused cell edge shrinkage. |
Co-immunoprecipitation, fusion protein forced localization, RNAi, cell migration assays, immunofluorescence |
PLoS biology |
Medium |
19492042
|
| 2009 |
Nudel is required for retrograde axonal transport in DRG neurons; anti-Nudel antibody injection abolishes retrograde transport of membranous organelles and leads to lysosome accumulation in axons and delayed endo-lysosome formation. |
Microinjection of blocking antibody into cultured DRG neurons, time-lapse microscopy, Golgi and lysosome localization assays |
Traffic |
Medium |
19522757
|
| 2010 |
Depletion of both NDE1 and NDEL1 causes striking dispersal of Golgi and endocytic organelles and complete loss of dynein from membranes. A substantial portion of NDE1 and NDEL1 is membrane-associated. NDE1 and NDEL1 act upstream of LIS1 in dynein recruitment on membrane: exogenous NDE1 or NDEL1 rescues LIS1 depletion effects on Golgi, while LIS1 only partially rescues loss of NDE1 and NDEL1. |
siRNA knockdown (single and double), organelle localization imaging, membrane fractionation, epistasis rescue experiments |
Journal of cell science |
High |
20048338
|
| 2010 |
Nudel/Ndel1 regulates microtubule organization during spindle assembly independently of kinetochore functions. Nudel directly interacts with lamin B to facilitate lamin-B-containing matrix accumulation and assembly on microtubules in a dynein-dependent manner. A novel dynein binding domain within the first 80 amino acids of Nudel was identified that interacts with dynein intermediate chain. |
Xenopus egg extract spindle assembly assay, immunodepletion, protein binding assays, extensive mutagenesis |
Nature cell biology / The Journal of biological chemistry |
High |
19198602 21056974
|
| 2010 |
Genetic mosaic analysis (MADM) established that Ndel1 is required cell-autonomously for a specific late step of neuronal migration: entry into the target lamina, distinct from Lis1's role in migration efficiency. |
Mosaic Analysis with Double Markers (MADM), in vivo sparse clonal analysis in mouse cortex |
Neuron |
High |
21092859
|
| 2011 |
Cdk5-phosphorylated Ndel1 promotes a high-affinity Lis1/Ndel1/dynein complex that blocks ATP-dependent release of dynein from microtubules, inhibiting processive motility. In adult axons, unphosphorylated Ndel1 inhibits dynein-mediated transport; Cdk5 phosphorylation of Ndel1 releases this inhibition and allows Lis1 to further stimulate cargo transport. |
RNAi, phosphorylation mutants, organelle transport assays in adult DRG axons, dominant-negative Cdk5 |
The Journal of neuroscience / Cell reports |
High |
22114287 26166569
|
| 2005 |
NUDEL possesses endooligopeptidase (cysteine protease) activity; mutation of Cys-273 fully abolishes this activity without disrupting secondary structure. DISC1 inhibits NUDEL-oligopeptidase activity in a competitive fashion, and the catalytic site is close to the DISC1-binding site on NUDEL. |
Site-directed mutagenesis of catalytic Cys-273, enzymatic activity assay, competitive inhibition assay |
Proceedings of the National Academy of Sciences of the United States of America |
High |
15728732
|
| 2010 |
The endooligopeptidase activity of Ndel1 is functionally important for neurite outgrowth in PC12 cells. Wild-type Ndel1 increases neurite-bearing cells; the catalytically dead mutant Ndel1(C273A) decreases neurite outgrowth; and RNAi depletion of Ndel1 is rescued by enzymatically active Ndel1(WT) but not Ndel1(C273A). |
RNAi, rescue with wild-type vs. catalytic mutant, neurite outgrowth quantification in PC12 cells |
Molecular and cellular neurosciences |
Medium |
20462516
|
| 2008 |
Ndel1 directly interacts with PDE4 family members, and the interaction with PDE4D3 is specifically disrupted by PKA phosphorylation at Ser13 of PDE4D3. Ndel1 sequesters EPAC (but not PKA) to form a cAMP signaling complex. Ndel1 self-interaction (dimerization) is stabilized by PDE4 binding. |
Co-immunoprecipitation, BRET interaction assay in living cells, peptide array mapping, PKA phosphorylation assay |
Cellular signalling |
Medium |
18845247
|
| 2011 |
PKA phosphorylates NDE1 at threonine-131 (T131) in a DISC1/PDE4-dependent manner. T131 phosphorylation modulates NDE1-LIS1 and NDE1-NDEL1 interactions, as confirmed by homology modeling and experimental binding assays. Mutation of T131 to mimic PKA phosphorylation inhibits neurite outgrowth. |
In vitro kinase assay, co-immunoprecipitation, homology modeling, neurite outgrowth assay, immunofluorescence |
The Journal of neuroscience |
Medium |
21677187
|
| 2012 |
Full-length NDEL1 forms dimers, tetramers, and chain-like polymers with a folded-back structure in solution. The C-terminal region, required for interaction with dynein and DISC1, folds back onto the N-terminal coiled-coil domain. NDE1 and NDEL1 can interact directly to form mixed complexes. |
Negative stain electron microscopy, chemical cross-linking/mass spectrometry, isotope labeling, biophysical characterization |
The Journal of biological chemistry |
High |
22843697
|
| 2012 |
Nudel directly interacts with misfolded Gβ (mfGβ) and recruits it to cytoplasmic dynein for transport to the centrosome/aggresome. Depletion of Nudel by RNAi reduces dynein-associated mfGβ, impairs aggresome formation, and prolongs the half-life of nascent Gβ. |
Co-immunoprecipitation, RNAi, half-life measurement, aggresome formation assay |
Cell research |
Medium |
22430153
|
| 2012 |
Nudel is crucial for in vivo assembly of the WAVE regulatory complex (WRC). Nudel stabilizes the Sra1-Nap1-Abi1 subcomplex through dynamic binding to Sra1 and protects HSPC300 from proteasomal degradation, stimulating HSPC300-WAVE2 complex formation. Depletion of Nudel abolishes WRC-dependent actin polymerization in vitro and Rac1-induced lamellipodial actin networks. |
Co-immunoprecipitation, RNAi, in vitro actin polymerization assay, cell spreading assay |
Cell research |
Medium |
22453242
|
| 2013 |
LIS1 is required for mitotic spindle organization via the LIS1-NDEL1-dynein complex. Overexpression of NDEL1-dynein and microtubule stabilization rescues spindle orientation defects in Lis1 mutants, placing NDEL1-dynein downstream of LIS1 in spindle orientation. |
Lis1 mutant mouse embryonic fibroblasts, time-lapse live cell imaging, rescue experiments, immunofluorescence |
Human molecular genetics |
Medium |
24030547
|
| 2013 |
Ndel1 and NudCL together regulate retrograde axonal mitochondrial transport. Knocking down both Ndel1 and NudCL almost blocks retrograde mitochondrial transport, while each alone only partially reduces it. LIS1 also interacts with KIF5b (kinesin) and its depletion suppresses mitochondrial motility in both anterograde and retrograde directions. |
siRNA knockdown (single and double), live imaging of mitochondrial transport in hippocampal neurons, co-immunoprecipitation |
Traffic |
Medium |
23551859
|
| 2016 |
NDEL1 localizes to the axon initial segment (AIS) via interaction with the scaffold protein Ankyrin-G. Depletion of NDEL1 or LIS1 results in non-polarized trafficking of dendritic cargo through the AIS. NDEL1 facilitates reversal of somatodendritic cargos in the proximal axon via local dynein activation. |
Co-immunoprecipitation, RNAi, live cargo tracking, immunofluorescence, fractionation |
Neuron |
High |
26844830
|
| 2016 |
Ndel1 localizes to the subdistal appendage of the mother centriole and suppresses primary cilia formation in proliferating cells by maintaining trichoplein at the mother centriole, thereby sustaining Aurora A activation. Serum starvation induces transient Ndel1 degradation followed by trichoplein disappearance and cilia assembly. Ndel1 acts upstream of the trichoplein-Aurora A pathway. |
siRNA knockdown, forced expression, immunofluorescence, mouse genetics (Ndel1 hypomorphic mice), co-localization studies |
The Journal of cell biology |
High |
26880200
|
| 2016 |
Ndel1 interacts with TRIO-associated repeat on actin (Tara), an actin-bundling protein. Loss of Ndel1 or Tara impairs cell migration. Tara overexpression induces accumulation of Ndel1 at the cell periphery co-localizing with F-actin. Co-expression of Ndel1 and Tara causes synergistic increase in F-actin and filopodia formation. |
Co-immunoprecipitation, RNAi, wound healing and Boyden chamber migration assays, immunofluorescence |
Scientific reports |
Medium |
27546710
|
| 2017 |
Crystal structure of DISC1 C-terminal tail in complex with Ndel1 binding domain was solved at high resolution. DISC1 regulates Ndel1 kinetochore attachment (but not centrosome localization) during mitosis. Disrupting DISC1/Ndel1 complex formation prolongs mitotic length and causes cell-cycle deficits in human cells and mouse cortical radial glia. |
X-ray crystallography, co-immunoprecipitation, live cell imaging, mouse in utero electroporation, human forebrain organoids, patient iPSCs |
Neuron |
High |
29103808
|
| 2019 |
Crystal structure of AnkB in complex with Ndel1 C-terminal coiled-coil (CT-CC) region revealed a stable 5-helix bundle with 2:1 (Ndel1:AnkB) stoichiometry. AnkG is essential for Ndel1 accumulation at the AIS. Cargo sorting at the AIS is disrupted by a peptide designed to block the AnkG/Ndel1 complex. |
X-ray crystallography, co-immunoprecipitation, live cargo tracking, peptide competition assay |
Proceedings of the National Academy of Sciences of the United States of America |
High |
31889000
|
| 2015 |
GSK-3β phosphorylates dynein intermediate chain (IC) at conserved residues S87/T88 (IC-1B) and S88/T89 (IC-2C) within the Ndel1-binding domain. This phosphorylation reduces IC interaction with Ndel1. Pharmacological or genetic inhibition of GSK-3β stimulates dynein motility. |
Co-immunoprecipitation, mass spectrometry, site-directed mutagenesis, in vitro phosphorylation assay, dynein motility assay |
Traffic |
Medium |
26010407
|
| 2015 |
DBZ (DISC1-binding zinc finger protein) hinders Ndel1 phosphorylation at Thr219 and Ser251. DBZ depletion or expression of double-phosphorylated Ndel1 impairs anterograde transport of Lis1 and DISC1 to neurite tips. This identifies a role for Ndel1 dual-phosphorylation state in regulating anterograde transport. |
RNAi, phosphomimetic expression, in utero electroporation, immunofluorescence, microtubule elongation assay |
The Journal of neuroscience |
Medium |
25698733
|
| 2017 |
NDEL1 is specifically S-nitrosylated at Cys203 by neuronal nitric oxide synthase (nNOS) in an NMDA receptor-activity-dependent manner. This S-nitrosylation accelerates dendritic arborization. Disruption of NDEL1 S-nitrosylation mediates impaired dendritic maturation caused by developmental alcohol exposure. |
Biotin-switch S-nitrosylation assay, site-directed mutagenesis of Cys203, genetic Nos1 deletion, NMDA receptor pharmacology, dendritic morphometry |
Cerebral cortex |
Medium |
27371763
|
| 2011 |
Ndel1 directly associates with Dynamin 2 (Dyn2) and enhances Dyn2 GTPase activity in its unassembled and assembled forms without promoting oligomerization. Gain and loss of function of Ndel1 recapitulate effects of Dyn2 overexpression or dominant-negative Dyn2 on intracellular localization of GluR1. |
Co-immunoprecipitation, in vitro GTPase activity assay, gain/loss-of-function experiments, GluR1 localization assay |
PloS one |
Medium |
21283621
|
| 2021 |
Ndel1 binds directly to keratin subunits through a motif conserved in all intermediate filament proteins and is necessary for robust desmosome-keratin association. Lis1 is required for desmosomal localization of Ndel1 but not for its effects on keratin filaments. Loss of Ndel1 in mouse epidermis results in desmosome defects. |
Direct binding assay, mouse genetics (conditional KO), immunofluorescence, desmosome morphology analysis |
Molecular biology of the cell |
Medium |
34319758
|
| 2023 |
The dynein intermediate chain N-terminus (ICN) is a critical evolutionarily conserved hub that interacts with both dynactin and Ndel1. Ndel1 recruits LIS1 to the dynein complex via ICN binding. LIS1 cannot simultaneously bind Ndel1 and dynein, requiring LIS1 to be handed off from Ndel1 to dynein in temporally discrete steps. In vitro, Ndel1 inhibits dynein activation by disfavoring dynein-dynactin-adaptor complex formation and by sequestering Lis1 away from dynein. Phosphomimetic C-terminal domain mutations in Ndel1 increase its ability to inhibit dynein-dynactin-adaptor complex formation. |
Purified protein binding assays, single-molecule imaging, in vitro reconstitution of dynein-dynactin-adaptor complex, mutagenesis |
Nature communications / The Journal of biological chemistry |
High |
37086789 37730751
|
| 2024 |
The NDEL1 variant p.R105P disrupts NDEL1 binding to LIS1, impairs neuronal migration, increases leading process length, and disrupts nucleus-centrosome coupling (nucleokinesis). This identifies the critical role of the LIS1-binding interface of NDEL1 in nucleokinesis during cortical development. |
In utero electroporation (mouse), single-cell RNA sequencing, spatial transcriptomics, biochemical binding assay, patient variant analysis |
Acta neuropathologica |
High |
38194050
|