ArticleMolecular biology of the cell2009
Interaction between Poly(ADP-ribose) and NuMA contributes to mitotic spindle pole assembly.
Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 85 citations in OpenAlex.
- Telomeres in mitosis: organization and dynamics.Nucleus (Austin, Tex.) · 2026Review
- The post-translational modification of NuMA in cancer cells is a new target for cancer eradication.Cell death & disease · 2025Review
- SASH1 S519N Variant Links Skin Hyperpigmentation and Premature Hair Graying to Dysfunction of Melanocyte Lineage.The Journal of investigative dermatology · 2025Article
- The role of Golgi complex proteins in cell division and consequences of their dysregulation.Frontiers in cell and developmental biology · 2024Review
- Tankyrase: a promising therapeutic target with pleiotropic action.Naunyn-Schmiedeberg's archives of pharmacology · 2023Review
- Multiple E3 ligases control tankyrase stability and function.Nature communications · 2023Article
- An Evolutionary Perspective on the Origin, Conservation and Binding Partner Acquisition of Tankyrases.Biomolecules · 2022Article
- A sePARate phase? Poly(ADP-ribose) versus RNA in the organization of biomolecular condensates.Nucleic acids research · 2022Review
- PARP10 Mediates Mono-ADP-Ribosylation of Aurora-A Regulating G2/M Transition of the Cell Cycle.Cancers · 2022Article
- The multi-functional RNA-binding protein G3BP1 and its potential implication in neurodegenerative disease.Journal of neurochemistry · 2021Review
- Thymoquinone-chemotherapeutic combinations: new regimen to combat cancer and cancer stem cells.Naunyn-Schmiedeberg's archives of pharmacology · 2020Review
- A FRET-based high-throughput screening platform for the discovery of chemical probes targeting the scaffolding functions of human tankyrases.Scientific reports · 2020Article
- Pleiotropic roles of tankyrase/PARP proteins in the establishment and maintenance of human naïve pluripotency.Experimental cell research · 2020Review
- Poly(ADP-ribose) polymerase enzymes and the maintenance of genome integrity.Cellular and molecular life sciences : CMLS · 2020Review
- Poly(ADP-Ribose) Glycohydrolase (PARG) vs. Poly(ADP-Ribose) Polymerase (PARP) - Function in Genome Maintenance and Relevance of Inhibitors for Anti-cancer Therapy.Frontiers in molecular biosciences · 2020Review
- Fragment-based screening identifies molecules targeting the substrate-binding ankyrin repeat domains of tankyrase.Scientific reports · 2019Article
- Targeting ADP-ribosylation as an antimicrobial strategy.Biochemical pharmacology · 2019Review
- Mitotic functions of poly(ADP-ribose) polymerases.Biochemical pharmacology · 2019Review
- RXXPEG motif of MERIT40 is required to maintain spindle structure and function through its interaction with Tankyrase1.Cell biology international · 2019Article
- Insights into the biogenesis, function, and regulation of ADP-ribosylation.Nature chemical biology · 2018Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Poly(ADP-ribose) (pADPr), made by PARP-5a/tankyrase-1, localizes to the poles of mitotic spindles and is required for bipolar spindle assembly, but its molecular function in the spindle is poorly understood. To investigate this, we localized pADPr at spindle poles by immuno-EM. We then developed a concentrated mitotic lysate system from HeLa cells to probe spindle pole assembly in vitro. Microtubule asters assembled in response to centrosomes and Ran-GTP in this system. Magnetic beads coated with pADPr, extended from PARP-5a, also triggered aster assembly, suggesting a functional role of the pADPr in spindle pole assembly. We found that PARP-5a is much more active in mitosis than interphase. We used mitotic PARP-5a, self-modified with pADPr chains, to capture mitosis-specific pADPr-binding proteins. Candidate binding proteins included the spindle pole protein NuMA previously shown to bind to PARP-5a directly. The rod domain of NuMA, expressed in bacteria, bound directly to pADPr. We propose that pADPr provides a dynamic cross-linking function at spindle poles by extending from covalent modification sites on PARP-5a and NuMA and binding noncovalently to NuMA and that this function helps promote assembly of exactly two poles.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.