Yeast Aim21/Tda2 both regulates free actin by reducing barbed end assembly and forms a complex with Cap1/Cap2 to balance actin assembly between patches and cables

Mol Biol Cell. 2018 Apr 15;29(8):923-936. doi: 10.1091/mbc.E17-10-0592. Epub 2018 Mar 30.

Abstract

Yeast Aim21 is recruited by the SH3-containing proteins Bbc1 and Abp1 to patches and, with Tda2, reduces barbed end assembly to balance the distribution of actin between patches and cables. Aim21/Tda2 also interacts with Cap1/Cap2, revealing a complex interplay between actin assembly regulators.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Actin Capping Proteins / genetics
  • Actin Capping Proteins / metabolism
  • Actin Cytoskeleton / metabolism*
  • Actins / metabolism*
  • Cytoskeletal Proteins / genetics
  • Cytoskeletal Proteins / metabolism
  • Endocytosis*
  • Genotype
  • Microfilament Proteins / genetics
  • Microfilament Proteins / metabolism*
  • Microscopy, Fluorescence
  • Models, Molecular
  • Mutation
  • Protein Binding
  • Protein Conformation
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Signal Transduction

Substances

  • ABP1 protein, S cerevisiae
  • Actin Capping Proteins
  • Actins
  • BBC1 protein, S cerevisiae
  • CAP1 protein, S cerevisiae
  • Cap2 protein, S cerevisiae
  • Cytoskeletal Proteins
  • Microfilament Proteins
  • Saccharomyces cerevisiae Proteins