ArticleThe Journal of biological chemistry2011
Molecular basis of actin nucleation factor cooperativity: crystal structure of the Spir-1 kinase non-catalytic C-lobe domain (KIND)•formin-2 formin SPIR interaction motif (FSI) complex.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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25 citing papers in PubMed, 35 citations in OpenAlex.
- The Cappuccino interactome reveals an intracellular role for Semaphorin-2a inbioRxiv : the preprint server for biology · 2026Article
- miR-379-5p promotes ovarian granulosa cell apoptosis in primary ovarian insufficiency by targeting KNDC1 and PEG10.Frontiers in genetics · 2026Article
- Actomyosin organelle functions of SPIRE actin nucleators precede animal evolution.Communications biology · 2024Article
- Discovery of Inhibitory Fragments That Selectively Target Spire2-FMN2 Interaction.Journal of medicinal chemistry · 2023Article
- The actin nucleator Spir-1 is a virus restriction factor that promotes innate immune signalling.PLoS pathogens · 2022Article
- Rab27a co-ordinates actin-dependent transport by controlling organelle-associated motors and track assembly proteins.Nature communications · 2020Article
- Spire stimulates nucleation by Cappuccino and binds both ends of actin filaments.Molecular biology of the cell · 2020Article
- Exploring the iceberg: Prospects of coordinated myosin V and actin assembly functions in transport processes.Small GTPases · 2019Review
- The WH2 Domain and Actin Nucleation: Necessary but Insufficient.Trends in biochemical sciences · 2016Review
- Role of the C-terminal Extension of Formin 2 in Its Activation by Spire Protein and Processive Assembly of Actin Filaments.The Journal of biological chemistry · 2016Article
- A mitochondria-anchored isoform of the actin-nucleating spire protein regulates mitochondrial division.eLife · 2015Article
- Baculovirus protein PK2 subverts eIF2α kinase function by mimicry of its kinase domain C-lobe.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Structure of a Bud6/Actin Complex Reveals a Novel WH2-like Actin Monomer Recruitment Motif.Structure (London, England : 1993) · 2015Article
- Membrane targeting of the Spir·formin actin nucleator complex requires a sequential handshake of polar interactions.The Journal of biological chemistry · 2015Article
- Biallelic truncating mutations in FMN2, encoding the actin-regulatory protein Formin 2, cause nonsyndromic autosomal-recessive intellectual disability.American journal of human genetics · 2014Article
- The role of formin tails in actin nucleation, processive elongation, and filament bundling.The Journal of biological chemistry · 2014Article
- KNDC1 knockdown protects human umbilical vein endothelial cells from senescence.Molecular medicine reports · 2014Article
- Spire and Formin 2 synergize and antagonize in regulating actin assembly in meiosis by a ping-pong mechanism.PLoS biology · 2014Article
- Ligand-induced activation of a formin-NPF pair leads to collaborative actin nucleation.The Journal of cell biology · 2013Article
- Drosophila homologues of adenomatous polyposis coli (APC) and the formin diaphanous collaborate by a conserved mechanism to stimulate actin filament assembly.The Journal of biological chemistry · 2013Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
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Abstract
The distinct actin nucleation factors of the Spir and formin subgroup families cooperate in actin nucleation. The Spir/formin cooperativity has been identified to direct two essential steps in mammalian oocyte maturation, the asymmetric spindle positioning and polar body extrusion during meiosis. Understanding the nature and regulation of the Spir/Fmn cooperation is an important requirement to comprehend mammalian reproduction. Recently we dissected the structural elements of the Spir and Fmn family proteins, which physically link the two actin nucleation factors. The trans-regulatory interaction is mediated by the Spir kinase non-catalytic C-lobe domain (KIND) and the C-terminal formin Spir interaction motif (FSI). The interaction inhibits formin nucleation activity and enhances the Spir activity. To get insights into the molecular mechanism of the Spir/Fmn interaction, we determined the crystal structure of the KIND domain alone and in complex with the C-terminal Fmn-2 FSI peptide. Together they confirm the proposed structural homology of the KIND domain to the protein kinase fold and reveal the basis of the Spir/formin interaction. The complex structure showed a large interface with conserved and positively charged residues of the Fmn FSI peptide mediating major contacts to an acidic groove on the surface of KIND. Protein interaction studies verified the electrostatic nature of the interaction. The data presented here provide the molecular basis of the Spir/formin interaction and give a first structural view into the mechanisms of actin nucleation factor cooperativity.
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