| 2008 |
HAUS6 (Dgt6) is a subunit of the augmin complex, a stable multi-protein complex of Dgt proteins required for centrosome-independent microtubule generation within the spindle; RNAi knockdown of each Dgt protein substantially reduces spindle microtubule generation, leading to reduced kinetochore fiber formation, chromosome misalignment, and spindle bipolarity defects, particularly in the absence of functional centrosomes. |
RNAi knockdown in Drosophila S2 cells, co-immunoprecipitation to show stable complex formation, live-cell and fixed imaging of spindle phenotypes |
The Journal of cell biology |
High |
18443220
|
| 2008 |
FAM29A (HAUS6 human homologue) promotes microtubule-dependent microtubule amplification by directly interacting with and recruiting the NEDD1–gamma-tubulin ring complex to spindle microtubules; depletion reduces spindle MT density, impairs kinetochore fiber formation, activates the spindle assembly checkpoint, and delays mitotic progression without affecting centrosome- or chromatin-based MT nucleation. |
siRNA knockdown, co-immunoprecipitation (FAM29A–NEDD1–gamma-tubulin), MT regrowth assay after nocodazole washout, immunofluorescence |
The Journal of cell biology |
High |
19029337
|
| 2009 |
Drosophila Dgt6 (HAUS6 orthologue) is primarily required for kinetochore fiber (k-fiber) formation; co-precipitates with Msps/XMAP215, D-TACC, gamma-tubulin, Ndc80, and Nuf2; kinetochore-driven k-fiber regrowth after cold exposure is severely impaired in Dgt6-depleted cells, placing Dgt6 at the intersection of MT nucleation/stabilization and Ndc80 complex-mediated kinetochore attachment. |
RNAi knockdown, co-immunoprecipitation, MT regrowth assay after cold-induced depolymerization, immunofluorescence of k-fiber markers |
Current biology : CB |
High |
19836241
|
| 2009 |
FAM29A (HAUS6) is regulated by Plk1: Plk1 recruits FAM29A to spindle microtubules, which in turn targets NEDD1 to the spindle; Plk1, FAM29A, and NEDD1 form three separate complexes in vivo rather than one single complex; altering FAM29A levels redistributes NEDD1 between the centrosomes and the spindle, demonstrating that FAM29A controls the partitioning of NEDD1 between these two mitotic structures. |
Co-immunoprecipitation, overexpression and knockdown with quantitative immunofluorescence of NEDD1 partitioning, epistasis with Plk1 |
Journal of cell science |
High |
19596795
|
| 2011 |
Aurora-A kinase directly binds and phosphorylates the Augmin subunit Hice1 at an N-terminal Ser/Thr-17-21 cluster; phospho-mimetic mutation at this cluster reduces Hice1 microtubule binding activity in vitro, diminishes Hice1 spindle localization, and decreases FAM29A (HAUS6) association with spindles, while phospho-deficient mutation permits intraspindle nucleation but delays spindle pole separation. |
In vitro kinase assay, phospho-specific antibody immunostaining, MT cosedimentation/binding assay, phospho-mimetic and phospho-deficient mutagenesis, live-cell imaging |
The Journal of biological chemistry |
High |
21705324
|
| 2017 |
Cross-linking mass spectrometry of in vivo Drosophila Augmin identified that Dgt6 (HAUS6 orthologue) directly binds the gamma-TuRC protein Dgp71WD (NEDD1 orthologue); this interaction is required for gamma-TuRC accumulation on the mitotic spindle but not for Augmin localization itself. |
Immuno-affinity purification of Augmin from Drosophila embryos, cross-linking/mass spectrometry, biochemical binding assays, in vivo rescue experiments in Drosophila embryo |
Biology open |
High |
28351835
|
| 2018 |
The inner nuclear membrane protein Samp1 co-precipitates with gamma-tubulin and the HAUS6 subunit of the Augmin complex in live cells, and Samp1 depletion reduces HAUS6 levels at the mitotic spindle, demonstrating that Samp1 is involved in recruiting HAUS6 and gamma-tubulin to the spindle. |
Co-immunoprecipitation from live cells, siRNA knockdown with quantitative immunofluorescence of HAUS6 at spindle, rescue by Samp1 overexpression |
Journal of cell science |
Medium |
29514856
|
| 2021 |
Conditional knockout of Haus6 in mouse apical neural progenitors causes spindle defects and mitotic delay, triggering massive p53-dependent apoptosis and aborting brain development; co-deletion of Trp53 rescues cell death but surviving progenitors display exacerbated mitotic errors, chromosomal defects, and increased DNA damage, showing that augmin/HAUS6 is essential for apical progenitor mitosis independent of p53 status. |
Conditional knockout mouse model, p53 co-deletion epistasis, live imaging, immunofluorescence of spindle markers and DNA damage |
eLife |
High |
34427181
|
| 2022 |
RNAi-mediated depletion of Dgt6 (HAUS6 Drosophila orthologue) causes a significant delay in kinetochore-driven microtubule regrowth (KDMTR) after colcemid-induced depolymerization in S2 cells, placing HAUS6/augmin as a positive regulator of kinetochore-driven spindle reassembly. |
RNAi reverse genetics, colcemid-induced MT depolymerization and regrowth assay, immunofluorescence quantification of KDMTR kinetics |
Cells |
Medium |
35883570
|
| 2022 |
HAUS6 knockdown in colorectal cancer cell lines suppresses cell proliferation and arrests cell cycle at G0/G1 by reducing p53 and p21 degradation (activating the p53/p21 pathway), while HAUS6 overexpression increases cell viability; these effects are observed both in vitro and in vivo xenograft models. |
siRNA knockdown, overexpression, cell viability/proliferation assays, flow cytometry cell cycle analysis, in vivo xenograft, western blot of p53/p21 protein levels |
Frontiers in cell and developmental biology |
Medium |
35096810
|
| 2024 |
HAUS6 is essential for spindle bipolarization in human oocytes; loss-of-function studies identified HAUS6 as required for the transition from multipolar intermediates (formed at minor poles from kinetochore clusters) to a bipolar spindle; mutations in HAUS6 were identified in infertile patients with oocyte or embryo defects. |
High-resolution live imaging in >1800 human oocytes, loss-of-function experiments, patient mutation identification |
Science (New York, N.Y.) |
Medium |
39172836
|
| 2025 |
Cryo-EM structure of an augmin subcomplex on the microtubule reveals that the conserved calponin-homology (CH) domain of Haus6 (HAUS6) directly contacts the MT lattice and is a bona fide MT binding site; the Haus6 CH domain increases augmin's affinity for MTs and, together with a second binding site in the disordered N-terminus of Haus8, establishes the shallow branch angle of newly nucleated microtubules. |
Cryo-electron microscopy structure determination, in vitro MT binding assays, mutagenesis of the CH domain |
Nature communications |
High |
41173848
|