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Phosphorylation of Arp2 is not essential for Arp2/3 complex activity in fission yeast

View ORCID ProfileAlexander E. Epstein, Sofia Espinoza-Sanchez, View ORCID ProfileThomas D. Pollard
doi: https://doi.org/10.1101/372706
Alexander E. Epstein
1Departments of Molecular Cellular and Developmental Biology, Yale University, PO Box 208103, New Haven, CT 06520-8103 USA
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Sofia Espinoza-Sanchez
2Departments of Molecular Biophysics and Biochemistry, Yale University, PO Box 208103, New Haven, CT 06520-8103 USA
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Thomas D. Pollard
1Departments of Molecular Cellular and Developmental Biology, Yale University, PO Box 208103, New Haven, CT 06520-8103 USA
2Departments of Molecular Biophysics and Biochemistry, Yale University, PO Box 208103, New Haven, CT 06520-8103 USA
3Department of Cell Biology, Yale University, PO Box 208103, New Haven, CT 06520-8103 USA
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  • For correspondence: thomas.pollard@yale.edu
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Abstract

LeClaire et al. presented evidence that phosphorylation of three sites on the Arp2 subunit activates Arp2/3 complex to nucleate actin filaments. We mutated the homologous residues of Arp2 (Y198, T233 and T234) in the fission yeast genome to amino acids that preclude or mimic phosphorylation. Arp2/3 complex is essential for the viability of fission yeast, yet strains unable to phosphorylate these sites grew normally. Y198F/T233A/T234A Arp2 was only nonfunctional if GFP-tagged, as observed by LeClaire et al. in Drosophila cells. Replacing both T233 and T234 with aspartic acid was lethal, suggesting that phosphorylation might be inhibitory. Nevertheless, blocking phosphorylation at these sites had the same effect as mimicking it: slowing assembly of endocytic actin patches. Mass spectrometry revealed phosphorylation at a fourth conserved Arp2 residue, Y218, but both blocking and mimicking phosphorylation of Y218 only slowed actin patch assembly slightly. Therefore, phosphorylation of Y198, T233, T234 and Y218 is not required for the activity of fission yeast Arp2/3 complex.

Summary Previous research concluded that phosphorylation at three sites on Arp2 is necessary to activate Arp2/3 complex. Epstein et al. make genomic substitutions blocking or mimicking phosphorylation to demonstrate that phosphorylation of these three sites does not regulate Arp2/3 complex in fission yeast.

  • Abbreviation List

    NPF
    nucleation promoting factor
    WASp
    Wiskott-Aldrich syndrome protein
    MD simulations
    molecular dynamics simulations
    NIK
    Nck-interacting kinase
    LC-MS/MS
    liquid chromatography-tandem mass spectrometry
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    Posted July 19, 2018.
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    Phosphorylation of Arp2 is not essential for Arp2/3 complex activity in fission yeast
    Alexander E. Epstein, Sofia Espinoza-Sanchez, Thomas D. Pollard
    bioRxiv 372706; doi: https://doi.org/10.1101/372706
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    Phosphorylation of Arp2 is not essential for Arp2/3 complex activity in fission yeast
    Alexander E. Epstein, Sofia Espinoza-Sanchez, Thomas D. Pollard
    bioRxiv 372706; doi: https://doi.org/10.1101/372706

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