Affinage

NEDD1

Protein NEDD1 · UniProt Q8NHV4

Length
660 aa
Mass
72.0 kDa
Annotated
2026-06-10
29 papers in source corpus 19 papers cited in narrative 19 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

NEDD1 (GCP-WD) is a WD40-repeat adaptor that targets the γ-tubulin ring complex (γ-TuRC) to microtubule-organizing sites and thereby controls γ-TuRC-dependent microtubule nucleation during cell division (PMID:16378099, PMID:16461362). It is a γ-TuRC-associated subunit whose depletion disperses γ-tubulin from the centrosome and abolishes centrosomal microtubule nucleation while leaving the γ-TuRC otherwise intact; γ-tubulin cannot reach the centrosome without NEDD1, but NEDD1 localizes independently, establishing it as the upstream attachment factor and also as a requirement for centriole duplication (PMID:16378099, PMID:16461362). Binding to the γ-TuRC is mediated by a C-terminal ~62-residue α-helical domain that directly contacts γ-tubulin and forms a stable tetramer (PMID:20224777); cryo-EM shows this tetrameric helical assembly inserts into the lumen of the γ-TuRC cone, anchored to GCP4/5/6 through MZT1–GCP3 subcomplexes, while its N-terminal WD40 β-propeller domains project outward toward microtubules (PMID:39574704). The WD40 domain binds directly inside the V-junction of Augmin, enhancing Augmin dimerization to create a platform for γ-TuRC recruitment and branched microtubule nucleation (PMID:41387433). NEDD1 function is governed by site-specific phosphorylation that partitions it among distinct nucleation pathways: Nek9 phosphorylates Ser377 to drive centrosomal recruitment downstream of Plk1 (PMID:22818914), Aurora A phosphorylates Ser405 to enable chromosome-proximal and central-spindle/midzone nucleation (PMID:23273898, PMID:31028180), and PLK4 phosphorylates Ser325 to promote SAS-6 binding and cartwheel-dependent centriole biogenesis (PMID:33351100); additional phosphosites near the γ-tubulin-binding domain tune the interaction and are modulated by CEP192 (PMID:22595525). Beyond mitosis, NEDD1 is essential for acentriolar spindle organization in oocytes, where its loss causes meiotic spindle defects and aneuploidy (PMID:20079731), and it localizes to the basal foot of ciliary basal bodies to organize microtubules in multiciliated cells [PMID:bio_10.1101_2025.09.04.674302].

Mechanistic history

Synthesis pass · year-by-year structured walk · 18 steps
  1. 2005 High

    Established that γ-TuRC recruitment to the centrosome requires a dedicated adaptor rather than being intrinsic to the complex, identifying NEDD1/GCP-WD as that attachment factor.

    Evidence siRNA depletion, dominant-negative inhibition, co-IP and microtubule nucleation assays in human cells

    PMID:16378099

    Open questions at the time
    • Did not define the structural basis of γ-TuRC binding
    • Mitotic phosphorylation requirement noted but kinases unidentified
  2. 2006 High

    Resolved the directionality of the targeting relationship—NEDD1 localizes independently of γ-tubulin but γ-tubulin depends on NEDD1—and extended NEDD1 function to centriole duplication.

    Evidence siRNA depletion and GFP-fusion dominant-negative overexpression in human cells with nucleation/duplication readouts

    PMID:16461362

    Open questions at the time
    • Mapped binding only to C-terminal half, not a defined motif
    • Mechanism linking NEDD1 to centriole duplication unresolved at this stage
  3. 2008 High

    Distinguished centrosomal from spindle-based recruitment by showing FAM29A (Augmin component) tethers the NEDD1–γ-tubulin complex to spindle microtubules for MT-dependent amplification.

    Evidence Co-IP, mass spectrometry, siRNA depletion and nocodazole washout regrowth assays

    PMID:19029337

    Open questions at the time
    • Direct NEDD1–Augmin interface not yet defined
    • Did not address how partitioning is regulated
  4. 2008 Medium

    Probed conservation of the targeting role across systems, finding NEDD1 in a non-γ-TuRC complex in Xenopus extracts and dispensable for centrosomal γ-tubulin targeting there, indicating context-dependent function.

    Evidence Immunodepletion and sucrose gradient fractionation of Xenopus egg extracts with nucleation assays

    PMID:18252801

    Open questions at the time
    • Partially contradicts human-cell targeting data
    • Basis of the species/system difference not resolved
  5. 2009 Medium

    Showed how NEDD1 distribution between centrosome and spindle is controlled, placing Plk1 upstream of both FAM29A-dependent spindle targeting and direct centrosomal recruitment.

    Evidence Co-IP defining three separate complexes plus siRNA depletion and immunofluorescence in mammalian cells

    PMID:19596795

    Open questions at the time
    • Direct Plk1 phosphosites on NEDD1 not mapped here
    • Single lab
  6. 2010 High

    Defined the molecular basis of γ-tubulin binding by reconstituting a direct interaction through a 62-residue C-terminal helical domain that forms a tetramer.

    Evidence In vitro binding, mutagenesis, CD spectroscopy and analytical ultracentrifugation with cellular localization

    PMID:20224777

    Open questions at the time
    • Quaternary arrangement within the intact γ-TuRC not visualized
    • Single lab
  7. 2010 Medium

    Extended NEDD1's role to acentriolar MTOCs, showing it is essential for meiotic spindle assembly and chromosome segregation fidelity in oocytes.

    Evidence siRNA knockdown in mouse oocytes with spindle, γ-tubulin, SAC and aneuploidy readouts

    PMID:20079731

    Open questions at the time
    • Pericentrin-dependence shown by localization, not mechanism
    • Single lab
  8. 2012 High

    Identified the kinase and site (Nek9–Ser377) coupling Plk1 signaling to centrosomal NEDD1/γ-tubulin recruitment, separating it from the Nek6/Nek7 branch.

    Evidence In vitro kinase assay, phospho-specific antibodies, mutagenesis, Xenopus extracts and mammalian-cell depletion

    PMID:22818914

    Open questions at the time
    • How Ser377 phosphorylation mechanistically enhances centrosome binding unclear
    • Single lab
  9. 2012 High

    Showed that a cluster of phosphosites near the γ-tubulin-binding domain fine-tunes the NEDD1–γ-tubulin interaction and that CEP192 modulates this mitotic phosphorylation.

    Evidence MS phosphosite mapping, serine-to-alanine mutagenesis, Co-IP and siRNA rescue in human cells

    PMID:22595525

    Open questions at the time
    • Responsible kinase(s) for the S557–S574 cluster not assigned
    • Single lab
  10. 2012 High

    Defined a spatially restricted nucleation pathway by showing Aurora A–Ser405 phosphorylation is specifically required for chromosome-proximal, RanGTP-driven nucleation but not centrosomal nucleation.

    Evidence In vitro kinase assay, phospho-specific antibodies, mutagenesis, Xenopus extract and human-cell rescue

    PMID:23273898

    Open questions at the time
    • How Ser405 selectively licenses non-centrosomal nucleation unresolved
  11. 2012 Medium

    Linked NEDD1 to PCM integrity by showing it recruits Cep57 to centrosomes, whose loss fragments the PCM and weakens nucleation.

    Evidence Co-IP and siRNA depletion with immunofluorescence in mammalian cells

    PMID:22508265

    Open questions at the time
    • No reciprocal IP reported
    • Direct binding interface undefined
    • Single lab
  12. 2019 Medium

    Extended the Aurora A–Ser405 axis to cytokinesis, showing this phosphorylation concentrates NEDD1 at the midzone for central spindle microtubule nucleation.

    Evidence Aurora A inhibition with phosphomimetic/phospho-null NEDD1 rescue in human cells

    PMID:31028180

    Open questions at the time
    • Midzone recruitment partner not identified
    • Single lab
  13. 2021 High

    Connected NEDD1 phosphorylation to centriole biogenesis by showing PLK4–Ser325 phosphorylation drives SAS-6 binding and cartwheel initiation.

    Evidence In vitro kinase assay, Co-IP, phosphomimetic/phospho-null mutagenesis and overexpression in human cells

    PMID:33351100

    Open questions at the time
    • Structural basis of phospho-NEDD1–SAS-6 binding not determined
    • Single lab
  14. 2022 Medium

    Directly visualized that Ser411 phosphorylation is required for branched microtubule nucleation and balances centrosome- versus chromosome-driven nucleation in spindle assembly.

    Evidence Phospho-variant stable HeLa lines and TIRF microscopy of MT branching in Xenopus egg extracts

    PMID:36318115

    Open questions at the time
    • Responsible kinase for Ser411 not identified
    • Single lab
  15. 2024 High

    Provided the structural model for how NEDD1 docks onto the γ-TuRC, showing a C-terminal tetrameric helical bundle in the cone lumen anchored via MZT1–GCP3 to GCP4/5/6 with WD40 domains projecting outward.

    Evidence Cryo-EM, AlphaFold modeling and biochemical pulldowns of NEDD1 mutants (preprint, published JCB 2025)

    PMID:39574704

    Open questions at the time
    • How phosphorylation modulates this docked state structurally unaddressed
    • Co-occupancy with CDK5RAP2 functional consequence unclear
  16. 2025 High

    Defined the WD40-domain interaction with Augmin at atomic resolution, showing it binds inside the Augmin V-junction and enhances dimerization to build a branching nucleation platform.

    Evidence Reconstitution of plant Augmin–NEDD1 complex, cryo-EM, crosslinking MS and evolutionary covariation

    PMID:41387433

    Open questions at the time
    • Demonstrated with plant Augmin; full human complex not reconstituted
    • Interplay with branching-specific phosphosites not tested
  17. 2025 Medium

    Identified a post-translational stability control whereby MZT1 suppresses NEDD1 ubiquitination, linking NEDD1 abundance to cancer cell proliferation and metabolic stress sensitivity.

    Evidence Ubiquitination assay, Co-IP, siRNA knockdown, Western blot and xenograft in gastric cancer cells

    PMID:40204068

    Open questions at the time
    • E3 ligase mediating NEDD1 ubiquitination not identified
    • Single lab
  18. 2025 Medium

    Extended NEDD1's microtubule-organizing role to differentiated cilia, localizing it to the basal foot of basal bodies where it is uniquely required for basal foot microtubule organization.

    Evidence Expansion microscopy 3D mapping and siRNA depletion in human airway multiciliated cells (preprint)

    PMID:bio_10.1101_2025.09.04.674302

    Open questions at the time
    • Preprint; not peer-reviewed
    • Recruitment mechanism to basal foot undefined

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the distinct phosphorylation events (Ser325, Ser377, Ser405, Ser411 and the S557–S574 cluster) are spatially and temporally integrated on a single NEDD1 molecule to switch between centrosomal, chromosomal, midzone, branching and centriolar nucleation pathways remains unresolved.
  • No single study resolves combinatorial phospho-state of NEDD1 in vivo
  • Kinases for several sites (S411, S557–S574 cluster) not all assigned
  • Structural effect of phosphorylation on γ-TuRC/Augmin docking not determined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 5 GO:0008092 cytoskeletal protein binding 3
Localization
GO:0005815 microtubule organizing center 4 GO:0005856 cytoskeleton 3 GO:0005929 cilium 1
Pathway
R-HSA-1640170 Cell Cycle 5 R-HSA-1852241 Organelle biogenesis and maintenance 3
Partners
CEP192CEP57FAM29A/HAUS6GCP4/TUBGCP4GCP6/TUBGCP6MZT1SAS-6TUBG1
Complex memberships
Augmin/HAUS complexγ-tubulin ring complex (γ-TuRC)

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2005 GCP-WD/NEDD1 is a subunit of the human γ-TuRC and acts as an attachment factor targeting the γ-TuRC to the centrosome and mitotic spindle; depletion of GCP-WD disperses the γ-TuRC from the centrosome and abolishes centrosomal microtubule nucleation, while leaving the γ-TuRC intact and able to bind microtubules. Mitotic phosphorylation of GCP-WD is separately required for γ-tubulin association with the spindle. siRNA depletion, dominant-negative inhibition, immunofluorescence, co-immunoprecipitation, microtubule nucleation assays in human cells Nature Cell Biology High 16378099
2006 NEDD1 is required for centrosomal targeting of the γ-TuRC and for centriole duplication; NEDD1 can target to the centrosome independently of γ-tubulin, but γ-tubulin cannot reach the centrosome without NEDD1. The C-terminal half of NEDD1 mediates binding to γ-TuRCs. siRNA depletion, GFP-fusion overexpression (dominant negative), immunofluorescence, centrosome microtubule nucleation assays in human cells The Journal of Cell Biology High 16461362
2008 FAM29A interacts with the NEDD1–γ-tubulin complex and recruits it to the mitotic spindle, promoting microtubule-dependent microtubule amplification and kinetochore fiber maturation. Co-immunoprecipitation, mass spectrometry, siRNA depletion, immunofluorescence, nocodazole washout microtubule regrowth assay The Journal of Cell Biology High 19029337
2008 Xenopus NEDD1 exists in a complex distinct from the γ-TuRC and is largely dispensable for targeting γ-tubulin to centrosomes in Xenopus egg extracts, but is required for microtubule organization in those extracts. Immunodepletion of Xenopus egg extracts, sucrose gradient fractionation, microtubule nucleation/organization assays Journal of Cell Science Medium 18252801
2009 FAM29A is regulated by Plk1, and Plk1, FAM29A, and NEDD1 form three separate complexes in vivo. Plk1 recruits FAM29A to spindle microtubules, which in turn targets NEDD1 to the spindle; Plk1 independently recruits NEDD1 to centrosomes. FAM29A controls partitioning of NEDD1 between centrosomes and spindle. Co-immunoprecipitation, siRNA depletion, immunofluorescence, overexpression studies in mammalian cells Journal of Cell Science Medium 19596795
2010 NEDD1 directly binds γ-tubulin through a 62-residue C-terminal helical domain that forms a stable tetramer in solution; mutation of residues in this domain disrupts γ-tubulin binding and causes mis-localization of γ-tubulin away from the centrosome. In vitro binding assays, site-directed mutagenesis, CD spectroscopy, analytical ultracentrifugation, immunofluorescence in mammalian cells PLoS ONE High 20224777
2010 NEDD1 is an essential component of acentriolar MTOCs in mouse oocytes, co-localizing with γ-tubulin and pericentrin in a pericentrin-dependent manner. NEDD1 knockdown reduces γ-tubulin at MTOCs, disrupts meiotic spindle structure, causes metaphase-I arrest via spindle checkpoint activation, and leads to high-frequency aneuploidy. siRNA knockdown in mouse oocytes, immunofluorescence, spindle checkpoint assay (MAD2 detection), chromosome segregation analysis 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 role of Nek9 requires Plk1-dependent activation of Nek9 but is independent of downstream kinases Nek6 and Nek7. In vitro kinase assay, phospho-specific antibodies, mutagenesis, Xenopus egg extracts, siRNA depletion in mammalian cells, immunofluorescence Current Biology High 22818914
2012 Multiple phosphorylation sites in the S557–S574 region of NEDD1, near its γ-tubulin-binding domain, finely tune the NEDD1–γ-tubulin interaction and spindle assembly. S565–S574 phosphorylation inhibits γ-tubulin binding; additional S557–T560 mutations restore binding. CEP192 associates with NEDD1 and modulates its mitotic phosphorylation. Mass spectrometry phosphosite mapping, serine-to-alanine mutagenesis, co-immunoprecipitation, siRNA rescue experiments, immunofluorescence Journal of Cell Science High 22595525
2012 Aurora A phosphorylates NEDD1 at Ser405, and this phosphorylation is specifically required for microtubule nucleation around chromosomes (not at centrosomes) and for RanGTP-driven aster formation in Xenopus egg extracts. In vitro kinase assay, phospho-specific antibodies, site-directed mutagenesis, Xenopus egg extract MT nucleation assays, siRNA rescue in human cells, immunofluorescence Current Biology High 23273898
2012 Cep57 interacts with NEDD1, and this interaction is required for centrosomal localization of Cep57. Loss of Cep57 causes PCM fragmentation, multipolar spindles, and weakened centrosomal microtubule nucleation. Co-immunoprecipitation, siRNA depletion, immunofluorescence in mammalian cells Cell Research Medium 22508265
2019 Aurora A phosphorylation of NEDD1 on Ser405 is required for NEDD1 concentration in the midzone during central spindle (cytokinetic spindle) assembly; a phosphomimetic NEDD1-S405E mutant rescues midzone microtubule nucleation under Aurora A inhibition. Aurora A inhibitor treatment, phosphomimetic/phospho-null NEDD1 mutant expression, immunofluorescence, microtubule nucleation assays in human cells Journal of Cell Science Medium 31028180
2021 PLK4 phosphorylates NEDD1 at Ser325, directly promoting NEDD1 binding to SAS-6 and recruitment of SAS-6 to the centrosome, thereby initiating cartwheel assembly and daughter centriole biogenesis. Phosphomimetic S325E promotes these initiations; non-phosphorylatable S325A abolishes them. In vitro kinase assay, co-immunoprecipitation, phosphomimetic/phospho-null mutagenesis, immunofluorescence, overexpression in human cells The Journal of Cell Biology High 33351100
2022 NEDD1 phosphorylation at S411 is essential for MT branching nucleation on pre-existing microtubules, demonstrated directly by TIRF microscopy in Xenopus egg extracts. S411 phosphorylation also coordinates the balance between centrosome- and chromosome-dependent MT nucleation required for bipolar spindle assembly. Stable inducible HeLa cell lines expressing phospho-variants, Xenopus egg extract TIRF microscopy of MT branching, immunofluorescence Biology Open Medium 36318115
2024 Cryo-EM structures of NEDD1 bound to the human γ-TuRC reveal that the C-terminus of NEDD1 forms a tetrameric α-helical assembly contacting the lumen of the γ-TuRC cone, anchored to GCP4, GCP5, and GCP6 via MZT1–GCP3 subcomplexes, with its microtubule-binding WD40 domains oriented away from the complex. NEDD1 does not induce conformational changes in the γ-TuRC. CDK5RAP2 and NEDD1 can simultaneously associate with the open conformation of the γ-TuRC. Cryo-EM structure determination, AlphaFold modeling, biochemical pulldown of NEDD1 mutants from cultured cells bioRxiv (preprint; published as JCB 2025 per PMID:39574704)preprint High 39574704
2025 MZT1 inhibits NEDD1 ubiquitination, thereby stabilizing NEDD1 protein levels in gastric cancer cells; MZT1 depletion reduces NEDD1 protein, decreasing proliferation and sensitizing cells to glucose starvation. Ubiquitination assay, co-immunoprecipitation, siRNA knockdown, Western blot, in vivo xenograft Life Sciences Medium 40204068
2025 The NEDD1 WD40 β-propeller domain binds directly inside the V-junction of Augmin, enhancing Augmin dimerization; this interaction, together with Augmin's dual CH-domain MT-binding, creates a platform for γ-TuRC recruitment and branched MT nucleation. Reconstitution of plant Augmin–NEDD1 complex, cryo-EM structure determination, crosslinking mass spectrometry, evolutionary covariation analysis Nature Communications High 41387433
2023 METTL3 promotes NEDD1 mRNA translation via YTHDF1-dependent m6A modification in DLBCL cells; NEDD1 in turn activates Hedgehog signaling to promote immune escape. meRIP-qPCR, dual-luciferase Hedgehog pathway assay, siRNA knockdown, overexpression, Western blot in DLBCL cell lines Immunity, Inflammation and Disease Low 36840486
2025 In human airway multiciliated cells, NEDD1 localizes to the basal foot of ciliary basal bodies and is essential for basal foot-dependent microtubule organization; depletion of NEDD1 (but not ninein or HAUS) disrupts this microtubule organization. Expansion microscopy 3D mapping, siRNA depletion, immunofluorescence in human airway multiciliated cells bioRxivpreprint Medium bio_10.1101_2025.09.04.674302

Source papers

Stage 0 corpus · 29 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 271 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 230 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
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 43 20224777
2012 Novel NEDD1 phosphorylation sites regulate γ-tubulin binding and mitotic spindle assembly. Journal of cell science 39 22595525
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 29 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

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