Affinage

HAUS5

HAUS augmin-like complex subunit 5 · UniProt O94927

Length
633 aa
Mass
71.7 kDa
Annotated
2026-06-10
6 papers in source corpus 2 papers cited in narrative 2 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 3/3 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

HAUS5 is a subunit of the Augmin/HAUS complex that functions in mitotic spindle assembly by coupling γ-tubulin-dependent microtubule nucleation to pre-existing spindle microtubules (PMID:28596487, PMID:28351835). HAUS5 is required for localization of the Augmin/HAUS complex to the mitotic spindle, and its loss causes mitotic arrest and centrosome fragmentation; HAUS5 acts downstream of ZNF131 in maintaining centrosome integrity, as ectopic HAUS5 rescues viability defects caused by ZNF131 knockdown (PMID:28596487). The Drosophila ortholog Dgt5 directly binds the γ-TuRC component Dgp71WD, an interaction required for accumulation of γ-TuRC—but not Augmin itself—at the spindle, defining HAUS5 as the Augmin element that recruits the γ-TuRC nucleation machinery (PMID:28351835). Beyond these functions, no further mechanistic detail has been characterized in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 2 steps
  1. 2017 Medium

    Established that HAUS5 is required to target the Augmin/HAUS complex to the mitotic spindle and to maintain centrosome integrity, and placed it within a ZNF131-regulated pathway.

    Evidence shRNA knockdown, ectopic overexpression rescue, and epistasis analysis with immunofluorescence of the mitotic spindle in glioblastoma stem-like cells

    PMID:28596487

    Open questions at the time
    • Mechanism by which ZNF131 regulates HAUS5 (transcriptional vs other) not directly demonstrated in this finding
    • Molecular basis for HAUS5-dependent spindle localization not resolved
    • Tested in a single cell type and single lab
  2. 2017 Medium

    Identified the direct molecular link between Augmin and the nucleation machinery by showing the HAUS5 ortholog Dgt5 binds the γ-TuRC component Dgp71WD to recruit γ-TuRC to the spindle.

    Evidence Cross-linking mass spectrometry of immunoaffinity-purified Drosophila Augmin, biochemical binding assays, and Drosophila embryo functional validation

    PMID:28351835

    Open questions at the time
    • Direct binding shown for the Drosophila ortholog, not validated for human HAUS5
    • No structural model of the Dgt5–Dgp71WD interface beyond XL-MS distance restraints
    • Whether this interaction underlies branched microtubule nucleation not directly tested here

Open questions

Synthesis pass · forward-looking unresolved questions
  • How HAUS5 within the human Augmin octamer engages γ-TuRC and is regulated to control branched nucleation in human mitosis remains undefined.
  • No human reconstitution of HAUS5-mediated γ-TuRC recruitment
  • No high-resolution structure of HAUS5 within the Augmin complex
  • Direct ZNF131–HAUS5 regulatory mechanism unconfirmed

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Pathway
R-HSA-1640170 Cell Cycle 2
Partners
DGP71WDHAUS2HAUS4
Complex memberships
Augmin/HAUS complex

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2017 HAUS5, a component of the Augmin/HAUS complex, is required for localization of the Augmin/HAUS complex to the mitotic spindle; its knockdown causes mitotic arrest, centrosome fragmentation, and loss of Augmin/HAUS complex on the mitotic spindle in glioblastoma stem-like cells (GSCs). Ectopic HAUS5 expression rescued viability defects caused by ZNF131 knockdown, placing HAUS5 downstream of ZNF131 in a pathway regulating centrosome integrity. shRNA knockdown, ectopic overexpression rescue, epistasis analysis (double knockdown with HAUS2/HAUS4), immunofluorescence of mitotic spindle Oncotarget Medium 28596487
2017 The Drosophila ortholog of HAUS5 (Dgt5) directly binds the γ-TuRC protein Dgp71WD, and this interaction is required for accumulation of γ-TuRC (but not Augmin itself) to the mitotic spindle; cross-linking/mass spectrometry identified distance restraints between Dgt5 and other Augmin subunits defining the interface. Cross-linking mass spectrometry (XL-MS) of immunoaffinity-purified Drosophila Augmin complex, biochemical binding assays, Drosophila embryo functional validation Biology open Medium 28351835

Source papers

Stage 0 corpus · 6 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
1995 Effect of competing self-structure on triplex formation with purine-rich oligodeoxynucleotides containing GA repeats. Nucleic acids research 78 7596824
2017 Cross-linking mass spectrometry identifies new interfaces of Augmin required to localise the γ-tubulin ring complex to the mitotic spindle. Biology open 22 28351835
2017 ZNF131 suppresses centrosome fragmentation in glioblastoma stem-like cells through regulation of HAUS5. Oncotarget 15 28596487
2010 Structure of the 1,N(2)-etheno-2'-deoxyguanosine lesion in the 3'-G(epsilon dG)T-5' sequence opposite a one-base deletion. Biochemistry 6 20201499
2003 Ethidium probing of the parallel double- and four-stranded structures formed by the telomeric DNA sequences dG(GT)4G and d(GT)5. Journal of biomolecular structure & dynamics 5 12744708
2024 SMA20/PMIS2 Is a Rapidly Evolving Sperm Membrane Alloantigen with Possible Species-Divergent Function in Fertilization. International journal of molecular sciences 1 38612464

Missed literature

Know a paper Affinage missed for HAUS5? Flag it for the maintainers and the community.

No submissions yet.