Understanding CRY2 interactions for optical control of intracellular signaling

Liting Duan, Jen Hope, Qunxiang Ong, Hsin-Ya Lou, Namdoo Kim, Comfrey McCarthy, Victor Acero, Michael Z. Lin () and Bianxiao Cui ()
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Liting Duan: Stanford University
Jen Hope: Stanford University
Qunxiang Ong: Stanford University
Hsin-Ya Lou: Stanford University
Namdoo Kim: Stanford University
Comfrey McCarthy: Northeastern University
Victor Acero: Pennsylvania State University
Michael Z. Lin: Stanford University
Bianxiao Cui: Stanford University

Nature Communications, 2017, vol. 8, issue 1, 1-10

Abstract: Abstract Arabidopsis cryptochrome 2 (CRY2) can simultaneously undergo light-dependent CRY2–CRY2 homo-oligomerization and CRY2–CIB1 hetero-dimerization, both of which have been widely used to optically control intracellular processes. Applications using CRY2–CIB1 interaction desire minimal CRY2 homo-oligomerization to avoid unintended complications, while those utilizing CRY2–CRY2 interaction prefer robust homo-oligomerization. However, selecting the type of CRY2 interaction has not been possible as the molecular mechanisms underlying CRY2 interactions are unknown. Here we report CRY2–CIB1 and CRY2–CRY2 interactions are governed by well-separated protein interfaces at the two termini of CRY2. N-terminal charges are critical for CRY2–CIB1 interaction. Moreover, two C-terminal charges impact CRY2 homo-oligomerization, with positive charges facilitating oligomerization and negative charges inhibiting it. By engineering C-terminal charges, we develop CRY2high and CRY2low with elevated or suppressed oligomerization respectively, which we use to tune the levels of Raf/MEK/ERK signaling. These results contribute to our understanding of the mechanisms underlying light-induced CRY2 interactions and enhance the controllability of CRY2-based optogenetic systems.

Date: 2017
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DOI: 10.1038/s41467-017-00648-8

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