A photoactivatable Src homology 2 (SH2) domain

Authors

• X. Song, University of Nebraska – Lincoln
• X. Shang, University of Nebraska – Lincoln
• T. Ju, University of Nebraska – Lincoln
• Ronald Cerny, University of Nebraska-LincolnFollow
• Wei Niu, University of Nebraska-LincolnFollow
• Jiantao Guo, University of Nebraska-LincolnFollow

Document Type

Article

Date of this Version

2016

Citation

RSC Adv., 2016, 6, 51120–51124

DOI: 10.1039/c6ra06211c

Comments

© The Royal Society of Chemistry 2016

Abstract

Src homology 2 (SH2) domains bind specifically to phosphotyrosine-containing motifs. As a regulatory module of intracellular signaling cascades, the SH2 domain plays important roles in the signal transduction of receptor tyrosine kinase pathways. In this work, we reported the construction of a photoactivatable SH2 domain through the combination of protein engineering and genetic incorporation of photo-caged unnatural amino acids. Significantly enhanced recognition of a phosphotyrosine-containing peptide substrate by the engineered SH2 domain mutant was observed after light-induced removal of the photo-caging group. Optical activation allows the control of protein and/or cellular function with temporal and spatial resolution. This photoactivatable SH2 domain could potentially be applied to the study of tyrosine phsophorylation-associated biological processes.