Affinage

NEDD1

Protein NEDD1 · UniProt Q8NHV4

Length
660 aa
Mass
72.0 kDa
Annotated
2026-04-29
31 papers in source corpus 20 papers cited in narrative 20 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

NEDD1 (GCP-WD) is a WD40-repeat adaptor protein that targets the γ-tubulin ring complex (γ-TuRC) to centrosomes, spindle microtubules, and acentrosomal nucleation sites, thereby governing microtubule nucleation in both mitosis and meiosis (PMID:16378099, PMID:16461362). Its C-terminal helical domain forms a tetramer that docks into the lumen of the γ-TuRC cone via MZT1–GCP3 modules anchored to GCP4/5/6, while its N-terminal WD40 β-propeller binds microtubules and the Augmin complex to support branched microtubule nucleation (PMID:39574704, PMID:41387433, PMID:36318115). NEDD1 function is regulated by sequential mitotic phosphorylation: Plk1→Nek9 phosphorylates S377 for centrosomal γ-TuRC recruitment, Aurora A phosphorylates S405 for chromosome-proximal and midzone microtubule nucleation, S411 phosphorylation drives microtubule branching, and PLK4 phosphorylates S325 to promote SAS-6 recruitment and centriole duplication (PMID:22818914, PMID:23273898, PMID:36318115, PMID:33351100). MZT1 stabilizes NEDD1 protein by inhibiting its ubiquitination, and loss of NEDD1 causes monopolar spindles, aneuploidy, and premature senescence (PMID:40204068, PMID:20079731, PMID:21364642).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 2005 High

    Before this work, it was unknown how the preassembled γ-TuRC reaches centrosomes; this study established that NEDD1 is a γ-TuRC subunit that functions as the essential attachment factor targeting γ-TuRC to centrosomes and mitotic chromatin for microtubule nucleation, and that mitotic phosphorylation regulates its spindle association separately from centrosomal localization.

    Evidence siRNA depletion, dominant-negative inhibition, immunoprecipitation, and γ-TuRC nucleation assays in human cells

    PMID:16378099

    Open questions at the time
    • Identity of the kinase(s) responsible for mitotic NEDD1 phosphorylation was unknown
    • Structural basis for NEDD1–γ-TuRC interaction unresolved
    • Mechanism of chromatin-mediated nucleation through NEDD1 not dissected
  2. 2006 High

    This work resolved the directionality of targeting: NEDD1 reaches centrosomes independently of γ-tubulin and then recruits γ-TuRC, and additionally showed that NEDD1 is required for centriole duplication, extending its role beyond microtubule nucleation.

    Evidence siRNA depletion, GFP-fusion localization, centrosome fractionation in human cells

    PMID:16461362

    Open questions at the time
    • Molecular basis of NEDD1 centrosomal targeting independent of γ-tubulin unknown
    • Whether NEDD1's centriole duplication role is direct or indirect through γ-tubulin was unclear
  3. 2008 High

    It was unclear how γ-TuRC is recruited to spindle microtubules for MT-dependent MT amplification; FAM29A was identified as the adaptor that recruits the NEDD1–γ-tubulin complex to the spindle, establishing a distinct pathway for kinetochore fiber maturation.

    Evidence Reciprocal co-immunoprecipitation, siRNA epistasis, live-cell imaging of spindle MT density

    PMID:19029337

    Open questions at the time
    • Upstream regulation of FAM29A–NEDD1 interaction unknown
    • Whether FAM29A and NEDD1 interact directly or through γ-TuRC was unresolved
  4. 2009 High

    Plk1 was shown to partition NEDD1 between the centrosome (direct Plk1–NEDD1 interaction) and the spindle (via Plk1-dependent FAM29A recruitment), revealing how a single kinase diversifies NEDD1 localization; separately, NEDD1 depletion phenotypes were shown to be p53-dependent, with monopolar spindles in p53-null cells and G1 arrest in p53-positive cells.

    Evidence Co-immunoprecipitation, siRNA/overexpression epistasis, Plk1 inhibitor BI2536, FACS analysis

    PMID:19243593 PMID:19596795

    Open questions at the time
    • Specific Plk1 phosphorylation site(s) on NEDD1 for centrosomal targeting not yet mapped
    • Mechanism linking NEDD1 loss to p53-dependent G1 arrest unresolved
  5. 2010 High

    The C-terminal γ-tubulin-binding domain of NEDD1 was structurally characterized as a 62-residue helical tetramer, and NEDD1 depletion in mouse oocytes and fibroblasts revealed meiotic aneuploidy and premature senescence, broadening the physiological impact of NEDD1 loss.

    Evidence In vitro binding, mutagenesis, structural characterization of C-terminal domain; siRNA in mouse oocytes and MEFs with chromosome segregation and senescence assays

    PMID:20079731 PMID:20224777 PMID:21364642

    Open questions at the time
    • Atomic-resolution structure of NEDD1 tetramer not determined
    • Whether the senescence phenotype is mediated by centrosome fragmentation or an independent pathway was unclear
  6. 2012 High

    Three distinct phosphoregulatory inputs were mapped: Nek9 phosphorylates S377 downstream of Plk1 for centrosomal γ-TuRC recruitment; Aurora A phosphorylates S405 specifically for chromatin-driven MT nucleation; and C-terminal phosphorylation at S565–S574 negatively regulates γ-tubulin binding, with CEP192 modulating this phosphorylation to control spindle assembly. Cep57 was also identified as a NEDD1-interacting PCM component.

    Evidence In vitro kinase assays, phospho-specific antibodies, phospho-mutant rescue in Xenopus extracts and mammalian cells, mass spectrometry phospho-mapping, co-immunoprecipitation

    PMID:22508265 PMID:22595525 PMID:22818914 PMID:23273898

    Open questions at the time
    • Kinase responsible for inhibitory S565–S574 phosphorylation unidentified
    • How CEP192 modulates NEDD1 phosphorylation mechanistically unknown
    • Whether Cep57–NEDD1 interaction is direct was not established
  7. 2015 Medium

    In developing neurons, loss of NEDD1 from centrosomes during maturation was shown to coincide with cessation of centrosomal MT nucleation, indicating that NEDD1 downregulation is a mechanism for the centrosome-to-acentrosomal MT nucleation switch during neuronal differentiation.

    Evidence Immunofluorescence in developing mouse brain sections, MT regrowth assays in cultured neurons

    PMID:26633906

    Open questions at the time
    • Whether NEDD1 loss is transcriptionally or post-translationally regulated during neuronal maturation is unknown
    • No causal manipulation (overexpression rescue) was performed
  8. 2019 Medium

    Aurora A–NEDD1 S405 phosphorylation was extended to central spindle assembly: this phosphoevent is required for midzone MT nucleation in late mitosis, broadening Aurora A–NEDD1 signaling beyond prophase/prometaphase.

    Evidence Aurora A inhibition with phosphomimetic NEDD1-S405 rescue, immunofluorescence of midzone assembly

    PMID:31028180

    Open questions at the time
    • Whether S405 phosphorylation is maintained throughout mitosis or re-phosphorylated at anaphase unknown
    • Independent replication in other systems needed
  9. 2021 High

    PLK4 was identified as a kinase that phosphorylates NEDD1-S325 to directly promote SAS-6 binding and centriole cartwheel assembly, establishing a direct mechanistic role for NEDD1 in centriole duplication initiation beyond γ-TuRC targeting.

    Evidence In vitro kinase assay, phosphomimetic/phospho-null mutant expression, co-immunoprecipitation, electron microscopy of cartwheel structures

    PMID:33351100

    Open questions at the time
    • Whether SAS-6 binds NEDD1 WD40 or C-terminal domain not mapped
    • Relationship between NEDD1-S325 phosphorylation and γ-TuRC function at the same centrosome unclear
  10. 2022 High

    S411 phosphorylation was shown to be specifically required for microtubule branching nucleation, directly visualized by TIRF microscopy, and to coordinate the balance between centrosome- and chromosome-dependent nucleation pathways.

    Evidence Phospho-variant HeLa lines, Xenopus egg extracts, TIRF microscopy of branching events

    PMID:36318115

    Open questions at the time
    • The kinase responsible for S411 phosphorylation was not identified
    • Whether S411 acts through Augmin/HAUS recruitment was not tested
  11. 2024 High

    Cryo-EM revealed how NEDD1 physically integrates into the γ-TuRC: its C-terminal tetramer occupies the lumen of the cone, anchored via MZT1–GCP3 to GCP4/5/6, while WD40 domains project outward; the γ-TuRC accommodates both NEDD1 and CDK5RAP2 simultaneously without conformational change.

    Evidence Cryo-EM structure determination with AlphaFold modeling and mutagenesis validation (preprint)

    PMID:39574704

    Open questions at the time
    • Full-length NEDD1 WD40 domain not resolved in cryo-EM density
    • Structural basis for phosphorylation-dependent regulation at individual sites not visualized
  12. 2025 Medium

    The WD40 domain of NEDD1 was shown to directly bind the Augmin V-junction and enhance Augmin dimerization, providing a structural basis for how NEDD1 anchors γ-TuRC to existing MTs for branched nucleation; separately, MZT1 was found to stabilize NEDD1 by inhibiting its ubiquitination.

    Evidence Cryo-EM of plant Augmin–NEDD1, crosslinking mass spectrometry, in vitro reconstitution; ubiquitination assays and tumor models for MZT1–NEDD1

    PMID:40204068 PMID:41387433

    Open questions at the time
    • Human Augmin–NEDD1 structural interaction not yet confirmed
    • Identity of the E3 ubiquitin ligase targeting NEDD1 unknown
    • Whether MZT1 stabilization of NEDD1 is relevant to normal mitotic regulation or primarily pathological contexts is unresolved

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key open questions include: the identity of the kinase(s) for S411 and the inhibitory S565–S574 cluster; an atomic-resolution structure of full-length NEDD1 including the WD40 domain bound to γ-TuRC; how the multiple phosphoregulatory inputs are spatiotemporally coordinated on a single NEDD1 molecule during mitosis; and whether NEDD1 mutations cause human disease.
  • No kinase identified for S411 or S565-S574
  • No full-length atomic structure of NEDD1 in complex
  • No human genetic disease linked to NEDD1 mutations

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4 GO:0008092 cytoskeletal protein binding 3
Localization
GO:0005815 microtubule organizing center 6 GO:0005856 cytoskeleton 4
Pathway
R-HSA-1640170 Cell Cycle 6 R-HSA-1852241 Organelle biogenesis and maintenance 3
Partners
AURKACEP192FAM29ANEK9PLK1PLK4SAS6TUBG1
Complex memberships
NEDD1–Augminγ-TuRC

Evidence

Reading pass · 20 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2005 NEDD1 (GCP-WD) is a subunit of the human γ-TuRC and acts as an attachment factor for the γ-TuRC: depletion or inhibition of NEDD1 causes loss of γ-TuRC from the centrosome, abolishing centrosomal microtubule nucleation, while leaving the γ-TuRC intact. NEDD1 depletion also blocks mitotic chromatin-mediated microtubule nucleation and spindle assembly. Mitotic phosphorylation of NEDD1 is required for association of γ-tubulin with the spindle (but separately from centrosomal association). siRNA depletion, dominant-negative inhibition, immunoprecipitation, γ-TuRC nucleation assays, mitotic phosphorylation analysis Nature cell biology High 16378099
2006 NEDD1 is required for centrosomal targeting of γ-TuRC: γ-TuRCs assemble normally without NEDD1 but cannot reach the centrosome. Conversely, NEDD1 targets to the centrosome independently of γ-tubulin. NEDD1 depletion impairs centriole duplication, as does depletion of γ-tubulin. The C-terminal half of NEDD1 mediates binding to γ-TuRC. siRNA depletion, GFP-fusion overexpression, immunofluorescence localization, centrosome fractionation The Journal of cell biology High 16461362
2008 FAM29A interacts with the NEDD1-γ-tubulin complex and recruits it to the mitotic spindle to promote MT-dependent MT amplification; NEDD1 is not required for centrosomal or chromatin-mediated nucleation per se, but its spindle recruitment by FAM29A is required for increasing MT mass and kinetochore fiber maturation. Co-immunoprecipitation, siRNA depletion, live-cell imaging, spindle MT density quantification The Journal of cell biology High 19029337
2009 FAM29A (a Plk1 substrate) controls the partitioning of NEDD1 between the centrosome and the mitotic spindle: Plk1 recruits FAM29A to spindle MTs, which in turn targets NEDD1 to the spindle; Plk1 recruits NEDD1 to centrosomes via a direct Plk1-NEDD1 interaction independent of FAM29A. Plk1, FAM29A, and NEDD1 form three separate complexes in vivo. Co-immunoprecipitation, siRNA depletion, overexpression, immunofluorescence Journal of cell science High 19596795
2010 NEDD1 directly binds γ-tubulin through a 62-residue C-terminal helical domain that forms a stable tetramer in solution. Mutations in this domain that disrupt γ-tubulin binding cause mis-localization of γ-tubulin away from the centrosome. NEDD1 is likely oligomeric in vivo. In vitro binding assay, mutagenesis, biochemical fractionation, immunofluorescence, structural characterization of C-terminal domain PloS one High 20224777
2010 NEDD1 co-localizes with γ-tubulin and pericentrin at MTOCs in mouse oocytes. NEDD1 depletion (siRNA) reduces γ-tubulin at MTOCs, disrupts meiotic spindle structure, causes metaphase-I arrest with spindle assembly checkpoint activation, and leads to 50% aneuploidy in oocytes that progress to metaphase-II. siRNA knockdown, immunofluorescence co-localization, MAD2 kinetochore staining, chromosome segregation assay Developmental biology Medium 20079731
2012 Nek9 phosphorylates NEDD1 on Ser377, driving recruitment of NEDD1 and thereby γ-tubulin to the centrosome in mitotic cells. This Nek9 function requires activation by Plk1-dependent phosphorylation of Nek9, but is independent of Nek6/Nek7, positioning Nek9 as an intermediary in the Plk1→Nek9→NEDD1(S377) pathway for centrosomal γ-tubulin recruitment during centrosome maturation. In vitro kinase assay, phospho-specific antibodies, Xenopus egg extracts, mammalian cell siRNA/overexpression, phospho-mutant analysis Current biology : CB High 22818914
2012 Aurora A interacts with and phosphorylates NEDD1 at Ser405. Ser405 phosphorylation is not required for centrosomal MT nucleation but is critical for MT nucleation in the vicinity of chromosomes and for RanGTP-dependent aster formation in Xenopus egg extracts, indicating Aurora A promotes chromatin-driven MT assembly specifically through NEDD1-S405 phosphorylation. In vitro kinase assay, phospho-mutant rescue, Xenopus egg extracts, RanGTP aster assay, siRNA in mammalian cells Current biology : CB High 23273898
2012 Phosphorylation of NEDD1 in the S565-S574 region (near the γ-tubulin-binding domain) inhibits NEDD1 binding to γ-tubulin and causes spindle assembly defects equivalent to NEDD1 depletion; additional mutations in S557-T560 restore γ-tubulin binding and bipolar spindle assembly. CEP192 associates with NEDD1 and modulates its mitotic phosphorylation, thereby regulating spindle assembly. Mass spectrometry phospho-site mapping, serine-to-alanine mutagenesis, Co-immunoprecipitation, spindle assembly assay Journal of cell science High 22595525
2012 Cep57 (a PCM component) interacts with NEDD1, and this interaction is necessary for centrosomal localization of Cep57. Depletion of Cep57 leads to PCM fragmentation, multipolar spindles, and reduced centrosomal microtubule nucleation activity. Co-immunoprecipitation, siRNA depletion, immunofluorescence, spindle assembly analysis Cell research Medium 22508265
2019 Aurora A-mediated phosphorylation of NEDD1 at Ser405 is required for microtubule nucleation during central spindle (midzone) assembly in late mitosis; expression of a phosphomimetic NEDD1-S405 isoform restores midzone MT nucleation when Aurora A is inhibited. Aurora A inhibition, phosphomimetic NEDD1 rescue, immunofluorescence of midzone assembly Journal of cell science Medium 31028180
2021 PLK4 phosphorylates NEDD1 at Ser325, which directly promotes NEDD1 binding to SAS-6 and recruiting SAS-6 to the centrosome. Phosphomimetic NEDD1-S325E promotes cartwheel assembly and daughter centriole biogenesis initiation, whereas non-phosphorylatable S325A abolishes these initiations. NEDD1 thus acts on the PCM layer to initiate centriole duplication under PLK4 regulation. In vitro kinase assay, phosphomimetic/phospho-null mutant overexpression, Co-immunoprecipitation, immunofluorescence, electron microscopy The Journal of cell biology High 33351100
2022 NEDD1-S411 phosphorylation is essential for MT branching nucleation (demonstrated directly by TIRF microscopy in Xenopus egg extracts) and plays a crucial role in coordinating the balance between centrosome- and chromosome-dependent MT nucleation pathways required for bipolar spindle assembly. Stable inducible HeLa cell lines expressing phospho-variants, Xenopus egg extracts, TIRF microscopy of MT branching Biology open High 36318115
2024 Cryo-EM structure of NEDD1 bound to human γ-TuRC reveals that the C-terminus of NEDD1 forms a tetrameric α-helical assembly that contacts the lumen of the γ-TuRC cone, is anchored to GCP4, 5 and 6 via MZT1 & GCP3 subcomplexes, and orients its N-terminal WD40 (microtubule-binding) domains away from the complex. NEDD1 does not induce conformational changes in the γ-TuRC, and the γ-TuRC can simultaneously bind both NEDD1 and CDK5RAP2 in the open conformation. NEDD1 mutants unable to pull-down γ-tubulin biochemically validated the structural model. Cryo-EM structure determination, AlphaFold modeling, co-immunoprecipitation mutagenesis validation bioRxiv (preprint, published as JCB 2025)preprint High 39574704
2025 NEDD1's WD40 β-propeller domain directly binds the V-junction of Augmin (plant ortholog, structurally conserved principle); NEDD1 binding to Augmin enhances Augmin's antiparallel dimerization, and cooperativity between NEDD1 WD40 and the Augmin dual CH domains may regulate MT lattice binding to anchor γ-TuRC for branched MT nucleation. Cryo-EM structure, crosslinking mass spectrometry, in vitro reconstitution, co-evolutionary analysis Nature communications Medium 41387433
2025 In human multiciliated airway cells, NEDD1 localizes to the basal foot of ciliary basal bodies together with γ-TuRC and Augmin/HAUS, and functional analysis shows NEDD1 (but not ninein or HAUS) is essential for basal foot-dependent microtubule organization. Expansion microscopy, 3D volumetric averaging, functional depletion analysis bioRxiv (preprint)preprint Medium bio_10.1101_2025.09.04.674302
2025 MZT1 inhibits NEDD1 ubiquitination, thereby increasing NEDD1 protein levels. This mechanism promotes gastric cancer cell resistance to glucose starvation and oncogenic behavior. Co-immunoprecipitation, ubiquitination assay, siRNA depletion, in vivo tumor model Life sciences Medium 40204068
2009 Silencing NEDD1 in p53-positive cells causes G1 arrest, whereas p53-negative cells arrest in mitosis with predominantly monopolar spindles; combining low-dose NEDD1 siRNA with the Plk1 inhibitor BI2536 synergistically arrests both cell types in mitosis, placing NEDD1 and Plk1 in a functionally cooperative pathway controlling mitotic entry. siRNA, pharmacological Plk1 inhibition (BI2536), FACS cell cycle analysis, immunofluorescence Molecular cancer Medium 19243593
2010 Depletion of NEDD1 in mouse embryonic fibroblasts causes centrosomal fragmentation and premature entry into senescence, linking centrosomal integrity (dependent on NEDD1) to suppression of the senescence program. siRNA depletion, centrosome immunofluorescence, senescence assays (β-galactosidase, BrdU) Cell death & disease Medium 21364642
2015 In developing mouse brain neurons, GCP-WD/NEDD1 and CDK5RAP2 are lost from centrosomes during neuron maturation, coinciding with loss of centrosomal γ-tubulin and cessation of centrosomal MT nucleation activity; MT nucleation subsequently occurs within dendrites rather than at the centrosome. Immunofluorescence in developing brain sections, RT-PCR, MT regrowth assay in cultured neurons Acta histochemica et cytochemica Medium 26633906

Source papers

Stage 0 corpus · 31 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2005 GCP-WD is a gamma-tubulin targeting factor required for centrosomal and chromatin-mediated microtubule nucleation. Nature cell biology 269 16378099
2006 NEDD1-dependent recruitment of the gamma-tubulin ring complex to the centrosome is necessary for centriole duplication and spindle assembly. The Journal of cell biology 228 16461362
2008 FAM29A promotes microtubule amplification via recruitment of the NEDD1-gamma-tubulin complex to the mitotic spindle. The Journal of cell biology 95 19029337
2009 The WD40 repeat protein NEDD1 functions in microtubule organization during cell division in Arabidopsis thaliana. The Plant cell 93 19383896
2012 Nek9 phosphorylation of NEDD1/GCP-WD contributes to Plk1 control of γ-tubulin recruitment to the mitotic centrosome. Current biology : CB 68 22818914
2012 The role of NEDD1 phosphorylation by Aurora A in chromosomal microtubule nucleation and spindle function. Current biology : CB 54 23273898
2010 NEDD1 is crucial for meiotic spindle stability and accurate chromosome segregation in mammalian oocytes. Developmental biology 52 20079731
2010 A direct interaction with NEDD1 regulates gamma-tubulin recruitment to the centrosome. PloS one 42 20224777
2012 Novel NEDD1 phosphorylation sites regulate γ-tubulin binding and mitotic spindle assembly. Journal of cell science 38 22595525
2014 GCP-WD mediates γ-TuRC recruitment and the geometry of microtubule nucleation in interphase arrays of Arabidopsis. Current biology : CB 31 25438942
2010 A potential role for NEDD1 and the centrosome in senescence of mouse embryonic fibroblasts. Cell death & disease 31 21364642
2012 Cep57, a NEDD1-binding pericentriolar material component, is essential for spindle pole integrity. Cell research 30 22508265
2006 NEDD1: function in microtubule nucleation, spindle assembly and beyond. The international journal of biochemistry & cell biology 28 17005434
2008 Xenopus NEDD1 is required for microtubule organization in Xenopus egg extracts. Journal of cell science 26 18252801
2015 Loss of γ-tubulin, GCP-WD/NEDD1 and CDK5RAP2 from the Centrosome of Neurons in Developing Mouse Cerebral and Cerebellar Cortex. Acta histochemica et cytochemica 23 26633906
2009 FAM29A, a target of Plk1 regulation, controls the partitioning of NEDD1 between the mitotic spindle and the centrosomes. Journal of cell science 21 19596795
2009 The centrosome protein NEDD1 as a potential pharmacological target to induce cell cycle arrest. Molecular cancer 20 19243593
2012 Intraperitoneal delivery of a small interfering RNA targeting NEDD1 prolongs the survival of scirrhous gastric cancer model mice. Cancer science 19 23106787
2021 PLK4-phosphorylated NEDD1 facilitates cartwheel assembly and centriole biogenesis initiations. The Journal of cell biology 16 33351100
2019 Microtubule nucleation during central spindle assembly requires NEDD1 phosphorylation on serine 405 by Aurora A. Journal of cell science 14 31028180
2010 An essential function for the centrosomal protein NEDD1 in zebrafish development. Cell death and differentiation 14 20150915
2008 Nedd1 expression as a marker of dynamic centrosomal localization during mouse embryonic development. Histochemistry and cell biology 14 18239929
1995 Assignment of the developmentally regulated gene NEDD1 to human chromosome 12q22 by fluorescence in situ hybridization. Human genetics 6 7814034
2024 NEDD1 overexpression increases cell proliferation, tumor immune escape, and drug resistance in LUAD. Journal of Cancer 5 38577589
2023 METTL3 enhances the effect of YTHDF1 on NEDD1 mRNA stability by m6A modification in diffuse large B-cell lymphoma cells. Immunity, inflammation and disease 5 36840486
2022 NEDD1-S411 phosphorylation plays a critical function in the coordination of microtubule nucleation during mitosis. Biology open 4 36318115
2025 Cryo-EM structures of the Plant Augmin reveal its intertwined coiled-coil assembly, antiparallel dimerization and NEDD1 binding mechanisms. bioRxiv : the preprint server for biology 1 40034650
2025 MZT1 protects gastric cancer against glucose starvation through targeting NEDD1. Life sciences 1 40204068
2024 Structure of the microtubule anchoring factor NEDD1 bound to the γ-tubulin ring complex. bioRxiv : the preprint server for biology 1 39574704
2025 Microtubule nucleation: How the NEDD1:MZT1:GCP3 trio captures the γ-TuRC. The Journal of cell biology 0 40663060
2025 Cryo-EM structures of plant Augmin reveal coiled-coil assembly, antiparallel dimerization, and NEDD1 binding. Nature communications 0 41387433