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.

Details

Title
Understanding CRY2 interactions for optical control of intracellular signaling
Author
Duan, Liting 1 ; Hope, Jen 1 ; Ong, Qunxiang 1 ; Hsin-Ya Lou 1 ; Kim, Namdoo 2 ; McCarthy, Comfrey 3 ; Acero, Victor 4 ; Lin, Michael Z 2   VIAFID ORCID Logo  ; Cui, Bianxiao 1 

 Department of Chemistry, Stanford University, Stanford, California, USA 
 Department of Bioengineering, Stanford University, Stanford, California, USA; Department of Pediatrics, Stanford University, Stanford, California, USA; Department of Neurobiology, Stanford University, Stanford, California, USA 
 Department of Psychology, Northeastern University, Boston, Massachusetts, USA 
 Department of Engineering Science, Pennsylvania State University, State College, Pennsylvania, USA 
Pages
1-10
Publication year
2017
Publication date
Sep 2017
Publisher
Nature Publishing Group
e-ISSN
20411723
Source type
Scholarly Journal
Language of publication
English
ProQuest document ID
1939221348
Copyright
© 2017. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.