| 1998 |
Mammalian NudC physically interacts with Lis1 (the lissencephaly gene product), demonstrated by yeast two-hybrid screen, in vitro protein-protein interaction assays, and co-immunoprecipitation from mouse brain extracts. |
Yeast two-hybrid screen, in vitro pulldown assay, co-immunoprecipitation from mouse brain extracts |
Current biology : CB |
High |
9601647
|
| 2001 |
NudC, Lis1, and cytoplasmic dynein intermediate chain (CDIC) colocalize at the MTOC at the leading pole of migrating cerebellar granule neurons; NudC co-immunoprecipitates with CDIC and cytoplasmic dynein heavy chain (CDHC) from mouse brain extracts, placing NudC in the dynein motor complex during neuronal migration. |
Immunofluorescence co-localization, co-immunoprecipitation from mouse brain extracts |
The Journal of neuroscience : the official journal of the Society for Neuroscience |
High |
11734602
|
| 2003 |
NudC plays roles in mitosis and cytokinesis; siRNA knockdown or adenoviral overexpression causes multinucleated cells, persistent intercellular connections, and disorganized midzone/midbody matrix. Polo-like kinase 1 (Plk1) is mislocalized from centrosomes and midbody when NudC levels are altered. In C. elegans, silencing of nud-1 (NudC ortholog) causes loss of midzone microtubules and cleavage furrow regression. |
siRNA knockdown, adenovirus-mediated overexpression, immunofluorescence microscopy, RNAi in C. elegans |
Journal of cell science |
High |
12679384
|
| 2003 |
NudC was identified as a Plk1 binding protein via cDNA phage display; Plk1 phosphorylates NudC at conserved S274 and S326 residues in vitro and in vivo. Rescue of NudC RNAi-induced cytokinesis defects (multinucleation, midbody arrest) requires wild-type NudC but not the S274A/S326A phosphorylation site mutant, establishing that Plk1 phosphorylation of NudC is functionally required for cytokinesis. |
cDNA phage display, in vitro kinase assay, in vivo phosphorylation assay, siRNA knockdown with rescue using phosphorylation-site mutants |
Developmental cell |
High |
12852857
|
| 2006 |
NudC is required for Plk1 targeting to kinetochores and chromosome congression. Plk1-phosphorylated NudC colocalizes with Plk1 at the outer kinetochore plate. NudC depletion reduces end-on microtubule attachments at kinetochores and mislocalizes Plk1 and CENP-E from prometaphase kinetochores. Rescue requires wild-type NudC but not the Plk1 phosphorylation-site mutant, establishing NudC as both substrate and spatial regulator of Plk1 at the kinetochore. |
siRNA knockdown, immunofluorescence microscopy, rescue with phosphorylation-site mutants |
Current biology : CB |
High |
16860740
|
| 2010 |
NudC functions as an Hsp90 co-chaperone to stabilize LIS1: NudC binds Hsp90, regulates Hsp90 ATPase activity, and possesses intrinsic chaperone activity. The L279P mutation (equivalent to the Aspergillus L146P temperature-sensitive mutation) impairs NudC chaperone function, reduces LIS1 protein levels, and causes LIS1-depletion-like cellular phenotypes. Hsp90 inhibition (geldanamycin/radicicol) decreases LIS1; ectopic Hsp90 partially rescues LIS1 degradation caused by NudC-L279P. |
Site-directed mutagenesis, ATPase activity assay, immunoprecipitation, pharmacological Hsp90 inhibition, Western blot |
The Journal of biological chemistry |
High |
20675372
|
| 2011 |
Crystal structure and NMR analysis show human NudC contains a CS domain (characteristic of Hsp90 co-chaperones and small heat shock proteins) and dimerizes via an N-terminal coiled coil. NudC (and NudCL, but not NudCL2) inhibits aggregation of several target proteins in chaperone assays consistent with Hsp90-independent heat shock protein function. However, none of the three NudC paralogs formed binary complexes with Lis1 in these assays. |
X-ray crystallography, NMR, in vitro aggregation assay |
Journal of molecular biology |
High |
21530541
|
| 2011 |
NudC is required for interkinetic nuclear migration in radial glial progenitors and for neuronal migration during neocorticogenesis in rat embryo, demonstrated by in utero electroporation of shRNAs and dominant-negative/wild-type NudC constructs. |
In utero electroporation, shRNA knockdown, overexpression of mutant forms in embryonic rat brain |
Developmental biology |
High |
21771589
|
| 2013 |
NudC is deacetylated during mitosis; K39 is an acetylation site on NudC. The acetylation-mimetic K39Q mutant fails to rescue mitotic phenotypes (chromosome misalignment, missegregation, reduced spindle width) caused by NudC knockdown, while the acetylation-defective K39R mutant rescues these defects. NudC co-localizes and co-immunoprecipitates with HDAC3 on the mitotic spindle; HDAC3 knockdown or inhibition increases NudC acetylation, identifying HDAC3 as a deacetylase for NudC. |
Mass spectrometry identification of acetylation site, site-directed mutagenesis with rescue assay, co-immunoprecipitation, pharmacological HDAC3 inhibition |
PloS one |
High |
24069238
|
| 2015 |
NudC binds to and stabilizes cofilin 1 (an actin dynamics regulator), thereby regulating actin organization and ciliogenesis. NudC depletion causes similar ciliary defects as cofilin 1 depletion (cilia elongation, increased ciliated cells, zebrafish curved body/pericardial edema/laterality defects). Ectopic cofilin 1 expression significantly reverses NudC depletion phenotypes, placing cofilin 1 downstream of NudC. |
Co-immunoprecipitation, siRNA knockdown, rescue experiments, zebrafish morpholino knockdown with phenotypic analysis |
Cell research |
High |
26704451
|
| 2015 |
EML4 directly interacts with NudC (interaction mediated by EML4's WD40 repeat and the C-terminus of NudC) and is required for loading NudC onto the mitotic spindle. In EML4-depleted cells, NudC fails to localize to the mitotic spindle, while NudC depletion does not affect EML4 localization. |
Mass spectrometry interactome screen, co-immunoprecipitation, siRNA knockdown, immunofluorescence microscopy |
Cell cycle (Georgetown, Tex.) |
Medium |
25789526
|
| 2016 |
Aurora B phosphorylates NudC at T40; NudC co-localizes and co-immunoprecipitates with Aurora B at the midbody during mitosis. Aurora B inhibition (ZM447439) reduces NudC phosphorylation in vivo. The T40D phospho-mimetic NudC fails to rescue cytokinesis defects (intercellular bridge elongation, sustained Aurora B activity, reduced abscission) caused by NudC depletion, while T40A rescues them, indicating that dynamic dephosphorylation at T40 is required for cytokinesis completion. |
In vivo kinase inhibition, site-directed mutagenesis with rescue assay, co-immunoprecipitation, immunofluorescence microscopy |
PloS one |
High |
27074040
|
| 2019 |
NudC interacts with rhodopsin and the small GTPase Rab11a in rod photoreceptors. NudC is required for disk formation and photoreceptor protein localization in rod outer segments, as demonstrated by transgenic tadpole studies with NudC shRNA knockdown and rescue with murine NudC. |
Co-immunoprecipitation, shRNA knockdown in transgenic tadpoles, rescue experiments |
FASEB journal : official publication of the Federation of American Societies for Experimental Biology |
Medium |
31022349
|
| 2021 |
NudC (as an Hsp90 co-chaperone) is required to stabilize filamin A; NudC interacts with filamin A (identified by IP-mass spectrometry). The chaperone-defective NudC-L279P mutant decreases filamin A protein levels, causes actin disorganization, and suppresses cell migration. Ectopic filamin A or Hsp90 reverses these defects, placing filamin A as an Hsp90/NudC client required for cell migration. |
Immunoprecipitation-mass spectrometry, Western blot, overexpression of NudC-L279P mutant, rescue with filamin A or Hsp90, pharmacological Hsp90 inhibition |
Frontiers in cell and developmental biology |
Medium |
34262899
|
| 2022 |
NudC acts as an essential transfer factor between the Hsp40/70 and Hsp90 chaperone systems: NudC interacts with Hsp40 within Hsp40-Hsp70-client complexes and displaces Hsp70; NudC then interacts with Hsp90, enabling direct transfer of Hsp40-bound clients to Hsp90 for further processing. NudC increases client activation in vitro and in cells and is essential for cellular viability. |
Biochemical reconstitution, co-immunoprecipitation, in vitro client activation assay, genetic depletion |
Molecular cell |
High |
35063133
|
| 2022 |
In zebrafish axon terminals, NudC acts as a chaperone for Lis1; loss of NudC function reduces Lis1 levels, causing dynein/dynactin accumulation and increased microtubule stability. Pharmacological dynein inhibition restores microtubule dynamics in nudc mutant axon terminals, placing excess dynein motor activity downstream of NudC/Lis1 depletion in microtubule regulation. |
Forward genetic screen, immunofluorescence, pharmacological dynein inhibition, Western blot in zebrafish |
iScience |
High |
36147950
|
| 2024 |
Conditional knockout of NudC in mouse rod photoreceptors causes rhodopsin and mitochondria mislocalization (consistent with dynein inhibition), increased phosphorylated cofilin 1 (implicating NudC in cofilin 1-mediated actin depolymerization), ultrastructural outer segment defects, and rapid photoreceptor cell death by 6 weeks. LIS1 levels were unaffected, indicating a LIS1-independent role of NudC in rods. |
Conditional CRISPR/Cas9 knockout in mouse rods, electroretinography, immunofluorescence, transmission electron microscopy, Western blot |
FASEB journal : official publication of the Federation of American Societies for Experimental Biology |
High |
38441532
|
| 2007 |
Mouse NudC interacts with the regulatory beta subunit of platelet-activating factor acetylhydrolase I (PAF-AH(I)) and increases PAF-AH(I) catalytic activity; this regulatory activity maps to the conserved C-terminal half of NudC. |
Co-immunoprecipitation, PAF-AH(I) enzymatic activity assay with NudC deletion constructs |
FEBS letters |
Medium |
17555748
|
| 2025 |
RNF41 (an E3 ubiquitin ligase) directly interacts with NudC, ubiquitinates NudC, and promotes its proteasomal degradation. Loss of RNF41 increases NudC stability, which enhances β-tubulin polymerization and promotes bladder cancer cell migration and invasion. |
Co-immunoprecipitation, ubiquitination assay, siRNA knockdown and overexpression, Western blot, in vitro migration assay |
Cell death & disease |
Medium |
40494872
|
| 1997 |
Rat NudC (c15/RnudC) functionally complements the Aspergillus nudC3 nuclear migration mutant and restores NudF protein levels, demonstrating functional conservation of the nuclear migration role and indicating that NudC acts upstream of NudF (Lis1 ortholog) in the nuclear distribution pathway. |
Functional complementation in Aspergillus nidulans nudC3 temperature-sensitive mutant |
Molecular endocrinology (Baltimore, Md.) |
High |
9013770
|
| 2010 |
Human NudC binds to the thrombopoietin receptor (Mpl) extracellular domain 1, specifically residues 206–251; two hydrophobic residues Leu228 and Leu230 are critical for hNUDC binding (identified by alanine replacement mutagenesis), and the WGSWS motif is required for hNUDC but not TPO binding. |
Yeast two-hybrid, co-immunoprecipitation, T7 phage display, ELISA binding assays, alanine scanning mutagenesis |
The Journal of biological chemistry |
Medium |
20529857
|
| 2020 |
NAGK (N-acetylglucosamine kinase) interacts with NudC and Lis1 in the dynein complex; NAGK-NudC-Lis1-dynein complexes are detected around nuclei and at leading poles of migrating cells. NAGK overexpression accelerates cell migration while NAGK knockdown delays it; a NAGK peptide from the NudC-interacting domain retards migration, placing the NAGK-NudC-Lis1-dynein complex at the nuclear envelope as a regulator of cell migration. |
Yeast two-hybrid, pulldown assay, immunocytochemistry, proximity ligation assay, wound healing assay, in utero electroporation, shRNA knockdown |
International journal of molecular sciences |
Medium |
33374456
|
| 2026 |
In Drosophila polyploid salivary gland cells, NudC depletion reduces ribosome abundance, impairs translation, decreases ribosomal RNA levels, and triggers a homeostatic transcriptional/translational upregulation of ribosome biogenesis factors. This role in ribosome biogenesis is independent of NudC's established function in dynein regulation. |
RNAi knockdown in Drosophila salivary glands, ribosome profiling, RNA quantification, immunofluorescence |
Open biology |
Medium |
42229917
|