ArticleMolecular biology of the cell2005
Cell polarity protein Spa2P associates with proteins involved in actin function in Saccharomyces cerevisiae.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Oligomerization and exocyst coupling underlie Spa2-mediated focusing of polarized growth in fission yeast.Journal of cell science · 2025Article
- Transient septin sumoylation steers a Fir1-Skt5 protein complex between the split septin ring.The Journal of cell biology · 2024Article
- A positive feedback loop involving the Spa2 SHD domain contributes to focal polarization.PloS one · 2022Article
- Article
- Orchestrated actin nucleation by theThe Journal of biological chemistry · 2020Article
- Spitzenkörper assembly mechanisms reveal conserved features of fungal and metazoan polarity scaffolds.Nature communications · 2020Article
- Polarisome scaffolder Spa2-mediated macromolecular condensation of Aip5 for actin polymerization.Nature communications · 2019Article
- YFR016c/Aip5 is part of an actin nucleation complex in yeast.Biology open · 2019Article
- Cell polarity protein Spa2 coordinates Chs2 incorporation at the division site in budding yeast.PLoS genetics · 2018Article
- A Predictive Model for Yeast Cell Polarization in Pheromone Gradients.PLoS computational biology · 2016Article
- Cell biology of yeast zygotes, from genesis to budding.Biochimica et biophysica acta · 2015Review
- The Cdc15 and Imp2 SH3 domains cooperatively scaffold a network of proteins that redundantly ensure efficient cell division in fission yeast.Molecular biology of the cell · 2015Article
- A protein complex containing Epo1p anchors the cortical endoplasmic reticulum to the yeast bud tip.The Journal of cell biology · 2015Article
- Identification of two tyrosine residues required for the intramolecular mechanism implicated in GIT1 activation.PloS one · 2014Article
- Yeast formin Bni1p has multiple localization regions that function in polarized growth and spindle orientation.Molecular biology of the cell · 2012Article
- Regulation of cell wall biogenesis in Saccharomyces cerevisiae: the cell wall integrity signaling pathway.Genetics · 2011Review
- Uncovering biological network function via graphlet degree signatures.Cancer informatics · 2008Article
- Yeast formins Bni1 and Bnr1 utilize different modes of cortical interaction during the assembly of actin cables.Molecular biology of the cell · 2007Article
- Functional characterization of Aspergillus nidulans homologues of Saccharomyces cerevisiae Spa2 and Bud6.Eukaryotic cell · 2006Article
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Authors and funding
6 authors.
Funding
Abstract
Spa2p is a nonessential protein that regulates yeast cell polarity. It localizes early to the presumptive bud site and remains at sites of growth throughout the cell cycle. To understand how Spa2p localization is regulated and to gain insight into its molecular function in cell polarity, we used a coimmunoprecipitation strategy followed by tandem mass spectrometry analysis to identify proteins that associate with Spa2p in vivo. We identified Myo1p, Myo2p, Pan1p, and the protein encoded by YFR016c as proteins that interact with Spa2p. Strikingly, all of these proteins are involved in cell polarity and/or actin function. Here we focus on the functional significance of the interactions of Spa2p with Myo2p and Myo1p. We find that localization of Spa2GFP to sites of polarized growth depends on functional Myo2p but not on Myo1p. We also find that Spa2p, like Myo2p, cosediments with F-actin in an ATP-sensitive manner. We hypothesize that Spa2p associates with actin via a direct or indirect interaction with Myo2p and that Spa2p may be involved in mediating polarized localization of polarity proteins via Myo2p. In addition, we observe an enhanced cell-separation defect in a myo1spa2 strain at 37 degrees C. This provides further evidence that Spa2p is involved in cytokinesis and cell wall morphogenesis.
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