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

被引：50

作者：

Anderson, Douglas P. ^{[1
,2
,3
]}

Whitney, Dustin S. ^{[4
]}

Hanson-Smith, Victor ^{[1
]}

Woznica, Arielle ^{[5
]}

Campodonico-Burnett, William ^{[2
,3
]}

Volkman, Brian F. ^{[4
]}

King, Nicole ^{[5
]}

Prehoda, Kenneth E. ^{[2
,3
]}

Thornton, Joseph W. ^{[6
,7
]}

机构：

[1] Univ Oregon, Inst Ecol & Evolut, Eugene, OR 97403 USA

[2] Univ Oregon, Dept Chem & Biochem, Eugene, OR 97403 USA

[3] Univ Oregon, Inst Mol Biol, Eugene, OR 97403 USA

[4] Med Coll Wisconsin, Dept Biochem, Milwaukee, WI 53226 USA

[5] Univ Calif Berkeley, Howard Hughes Med Inst, Dept Mol & Cellular Biol, Berkeley, CA 94720 USA

[6] Univ Chicago, Dept Ecol & Evolut, Chicago, IL 60637 USA

[7] Univ Chicago, Dept Human Genet, Chicago, IL 60637 USA

来源：

ELIFE | 2016年 / 5卷

关键词：

D O I：

10.7554/eLife.10147

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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 (GK(PID)) 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 GK(PID)'s capacity to bind the cortical marker protein can be recapitulated by reintroducing a single historical substitution into the reconstructed ancestral GK(PID). 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.

引用

页数：21