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Light regulation of protein dimerization and kinase activity in living cells using photocaged rapamycin and engineered FKBP.

ABSTRACT: We developed a new system for light-induced protein dimerization in living cells using a photocaged analogue of rapamycin together with an engineered rapamycin binding domain. Using focal adhesion kinase as a target, we demonstrated successful light-mediated regulation of protein interaction and localization in living cells. Modification of this approach enabled light-triggered activation of a protein kinase and initiation of kinase-induced phenotypic changes in vivo.

SUBMITTER: Karginov AV

PROVIDER: S-EPMC3133816 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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Light regulation of protein dimerization and kinase activity in living cells using photocaged rapamycin and engineered FKBP.

Karginov Andrei V AV Zou Yan Y Shirvanyants David D Kota Pradeep P Dokholyan Nikolay V NV Young Douglas D DD Hahn Klaus M KM Deiters Alexander A

Journal of the American Chemical Society 20101216 3

We developed a new system for light-induced protein dimerization in living cells using a photocaged analogue of rapamycin together with an engineered rapamycin binding domain. Using focal adhesion kinase as a target, we demonstrated successful light-mediated regulation of protein interaction and localization in living cells. Modification of this approach enabled light-triggered activation of a protein kinase and initiation of kinase-induced phenotypic changes in vivo. ...[more]

PMID: 21162531

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