Modulation of Light-Sensitive Homo-Oligomerization of CryptoChrome 2
Victor Acero , Liting Duan , Jen Hope , Bianxiao Cui
Background
Drugs are used to study important
protein-protein interactions
Low Spatiotemporal resolution
Cryptochrome2 (CRY2), can undergo
both light-induced homo-
oligomerization and hetero-
dimerization with its partner CIBN.
CRY2 Optogenetic Tool
Homo-Oligomerization Hetero-Dimerization
OFF ON OFF
DARK
Goals of Modulation
Preliminary Work
1.
2. Fluorescent tags have unique
multimeric properties. There is
a possibility they impact CRY2
Homo-Oligomerization.
1 2 2 2
The Pennsylvania State University , Stanford University
1 2
Multimeric Fusion Proteins Modulate CRY2 Homo-Oligomerization Conclusions
Fluorescent Tags
Multimeric properties of fusion
proteins, such as fluorescent tags,
will impact CRY2 homo-
oligomerization.
mCherry fused to CRY2 to
drastically increase homo-
oligomerization
B D
GFP fused to CRY2 will not
increase homo-oligomerization
ON Bulky Proteins
Multimeric properties of mCherry Demonstrated that tdTomato, a
will induce greater CRY2 nonfunctional protein, can be used to
DARK
oligomerization than GFP sterically hinder CRY2 homo-
oligomerization
Bulky proteins can be located on
Bulky Proteins Hinder CRY2 Homo-Oligomerization either CIBN or CRY2s N/C
F CRY2-tdTomato G tdTomato-CRY2 terminals to have a hindering
effect
Future Work
1. Develop a model to describe the
mechanism of CRY2 Homo-
Oligomerization
Fluorescent
Tags Modulate
Homo-
Oligomerization
Bulky Proteins
Sterically Hinder
Homo- ???
Oligomerization
Mechanisms of
Oligomerization
2. Characterize More Fluorescent Tags
Acknowledgements
Stanford University: Chemistry Department
Stanford Summer Research Program (2016)
Academic advising and professional development
Cui Lab Dr. Bianxiao Cui
Liting Duan and Jen Hope are responsible for my
introduction to optogenetics and guided my research.
Amgen Incorporated
>
Financial support for research, travel, and cost of
living