Medical College of Wisconsin
CTSICores SearchResearch InformaticsREDCap

Evolution of an ancient protein function involved in organized multicellularity in animals. Elife 2016 Jan 07;5:e10147

Date

01/08/2016

Pubmed ID

26740169

Pubmed Central ID

PMC4718807

DOI

10.7554/eLife.10147

Scopus ID

2-s2.0-84956891086   31 Citations

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.

Author List

Anderson DP, Whitney DS, Hanson-Smith V, Woznica A, Campodonico-Burnett W, Volkman BF, King N, Thornton JW, Prehoda KE

Author

Brian F. Volkman PhD Professor in the Biochemistry department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Animals
Cell Cycle
Cell Cycle Proteins
Evolution, Molecular
Guanylate Kinases
Models, Molecular
Protein Binding
Protein Multimerization
Spindle Apparatus
jenkins-FCD Prod-444 eb4ebd1a08581aba961d3befd3b851a3c3ec6b46