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Evolution of an ancient protein function involved in organized multicellularity in animals.

  • Author(s): Anderson, Douglas P
  • Whitney, Dustin S
  • Hanson-Smith, Victor
  • Woznica, Arielle
  • Campodonico-Burnett, William
  • Volkman, Brian F
  • King, Nicole
  • Thornton, Joseph W
  • Prehoda, Kenneth E
  • et al.
Abstract

To form and maintain organized tissues, multicellular organisms orient their mitotic spindles relative to neighboring cells. A molecular complex scaffolded by the GK protein-interaction domain (GKPID) mediates spindle orientation in diverse animal taxa by linking microtubule motor proteins to a marker protein on the cell cortex localized by external cues. Here we illuminate how this complex evolved and commandeered control of spindle orientation from a more ancient mechanism. The complex was assembled through a series of molecular exploitation events, one of which - the evolution of GKPID's capacity to bind the cortical marker protein - can be recapitulated by reintroducing a single historical substitution into the reconstructed ancestral GKPID. This change revealed and repurposed an ancient molecular surface that previously had a radically different function. We show how the physical simplicity of this binding interface enabled the evolution of a new protein function now essential to the biological complexity of many animals.

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