ArticleThe Journal of biological chemistry2009
The PN2-3 domain of centrosomal P4.1-associated protein implements a novel mechanism for tubulin sequestration.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 50 citations in OpenAlex.
- Epigenetic Regulation of Chromosomal Instability by EZH2 Methyltransferase.Cancer discovery · 2026Article
- Centriolar cap proteins CP110 and CPAP control slow elongation of microtubule plus ends.The Journal of cell biology · 2025Article
- Structural convergence for tubulin binding of CPAP and vinca domain microtubule inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- CPAP insufficiency leads to incomplete centrioles that duplicate but fragment.The Journal of cell biology · 2022Article
- Article
- Article
- Inhibition of CPAP-tubulin interaction prevents proliferation of centrosome-amplified cancer cells.The EMBO journal · 2019Article
- Review
- Interaction between theMolecular biology of the cell · 2018Article
- The ABCs of Centriole Architecture: The Form and Function of Triplet Microtubules.Cold Spring Harbor symposia on quantitative biology · 2017Article
- Fidgetin-like 1 is a ciliogenesis-inhibitory centrosome protein.Cell cycle (Georgetown, Tex.) · 2016Article
- Molecular basis for CPAP-tubulin interaction in controlling centriolar and ciliary length.Nature communications · 2016Article
- Centriolar CPAP/SAS-4 Imparts Slow Processive Microtubule Growth.Developmental cell · 2016Article
- Cenpj/CPAP regulates progenitor divisions and neuronal migration in the cerebral cortex downstream of Ascl1.Nature communications · 2015Article
- The centrosome and its duplication cycle.Cold Spring Harbor perspectives in biology · 2015Review
- Biochemical and structural insights into microtubule perturbation by CopN from Chlamydia pneumoniae.The Journal of biological chemistry · 2014Article
- Microcephaly genes evolved adaptively throughout the evolution of eutherian mammals.BMC evolutionary biology · 2014Article
- Cell Cycle Regulation of the Centrosome and Cilium.Drug discovery today. Disease mechanisms · 2013Article
- Structural analysis of the G-box domain of the microcephaly protein CPAP suggests a role in centriole architecture.Structure (London, England : 1993) · 2013Article
- Building a centriole.Current opinion in cell biology · 2013Review
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microtubules are cytoskeletal components involved in multiple cell functions such as mitosis, motility, or intracellular traffic. In vivo, these polymers made of alphabeta-tubulin nucleate mostly from the centrosome to establish the interphasic microtubule network or, during mitosis, the mitotic spindle. Centrosomal P4.1-associated protein (CPAP; also named CENPJ) is a centrosomal protein involved in the assembly of centrioles and important for the centrosome function. This protein contains a microtubule-destabilizing region referred to as PN2-3. Here we decrypt the microtubule destabilization activity of PN2-3 at the molecular level and show that it results from the sequestration of tubulin by PN2-3 in a non-polymerizable 1:1 complex. We also map the tubulin/PN2-3 interaction both on the PN2-3 sequence and on the tubulin surface. NMR and CD data on free PN2-3 in solution show that this is an intrinsically unstructured protein that comprises a 23-amino acid residue alpha-helix. This helix is embedded in a 76-residue region that interacts strongly with tubulin. The interference of PN2-3 with well characterized tubulin properties, namely GTPase activity, nucleotide exchange, vinblastine-induced self-assembly, and stathmin family protein binding, highlights the beta subunit surface located at the intermolecular longitudinal interface when tubulin is embedded in a microtubule as a tubulin/PN2-3 interaction area. These findings characterize the PN2-3 fragment of CPAP as a protein with an unprecedented tubulin sequestering mechanism distinct from that of stathmin family proteins.
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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.