A photoactivatable Src homology 2 (SH2) domain

X. Song, X. Shang, T. Ju, Ronald Cerny, Wei Niu, Jiantao Guo

Research output: Contribution to journalArticle

2 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)51120-51124
Number of pages5
JournalRSC Advances
Volume6
Issue number56
DOIs
StatePublished - Jan 1 2016

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Phosphotyrosine
Proteins
Signal transduction
Receptor Protein-Tyrosine Kinases
Peptides
Tyrosine
Amino acids
Chemical activation
Amino Acids
Substrates

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

Cite this

A photoactivatable Src homology 2 (SH2) domain. / Song, X.; Shang, X.; Ju, T.; Cerny, Ronald; Niu, Wei; Guo, Jiantao.

In: RSC Advances, Vol. 6, No. 56, 01.01.2016, p. 51120-51124.

Research output: Contribution to journalArticle

Song, X. ; Shang, X. ; Ju, T. ; Cerny, Ronald ; Niu, Wei ; Guo, Jiantao. / A photoactivatable Src homology 2 (SH2) domain. In: RSC Advances. 2016 ; Vol. 6, No. 56. pp. 51120-51124.
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