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

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 mark...

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Bibliographic Details
Main Authors: Douglas P Anderson, Dustin S Whitney, Victor Hanson-Smith, Arielle Woznica, William Campodonico-Burnett, Brian F Volkman, Nicole King, Joseph W Thornton, Kenneth E Prehoda
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2016-01-01
Series:eLife
Subjects:
Online Access:https://elifesciences.org/articles/10147
Description
Summary: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.
ISSN:2050-084X