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A photocleavable rapamycin conjugate for spatiotemporal control of small GTPase activity.


ABSTRACT: We developed a novel method to spatiotemporally control the activity of signaling molecules. A newly synthesized photocaged rapamycin derivative induced rapid dimerization of FKBP (FK-506 binding protein) and FRB (FKBP-rapamycin binding protein) upon UV irradiation. With this system and the spatially confined UV irradiation, we achieved subcellularly localized activation of Rac, a member of small GTPases. Our technique offers a powerful approach to studies of dynamic intracellular signaling events.

SUBMITTER: Umeda N 

PROVIDER: S-EPMC3850177 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

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A photocleavable rapamycin conjugate for spatiotemporal control of small GTPase activity.

Umeda Nobuhiro N   Ueno Tasuku T   Pohlmeyer Christopher C   Nagano Tetsuo T   Inoue Takanari T  

Journal of the American Chemical Society 20101213 1


We developed a novel method to spatiotemporally control the activity of signaling molecules. A newly synthesized photocaged rapamycin derivative induced rapid dimerization of FKBP (FK-506 binding protein) and FRB (FKBP-rapamycin binding protein) upon UV irradiation. With this system and the spatially confined UV irradiation, we achieved subcellularly localized activation of Rac, a member of small GTPases. Our technique offers a powerful approach to studies of dynamic intracellular signaling even  ...[more]

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