4.5 Article

Phototropin receptor kinase activation by blue light

Journal

PLANT SIGNALING & BEHAVIOR
Volume 3, Issue 1, Pages 44-46

Publisher

TAYLOR & FRANCIS INC
DOI: 10.4161/psb.3.1.4848

Keywords

phototropin; LOV domain; FMN; cysteinyl adduct; amphipathic helix; receptor autophosphoryation

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Phototropins (phot1 and phot2) are blue light-activated serine/threonine protein kinases that function to mediate a variety of adaptive processes that serve to optimize the photosynthetic efficiency of plants and thereby promote their growth. Light sensing by the phototropins is mediated by a repeated motif located within the N-terminal region of the protein designated the LOV domain. Although phototropins possess two LOV photosensors (LOV1 and LOV2), recent biophysical and structure-function analyses clearly indicate that the LOV2 domain plays a predominant role in regulating phototropin kinase activity owing to specific protein changes that occur in response to LOV2 photoexcitation. In particular, the central b-sheet scaffold plays a role in propagating the photochemical signal generated from within LOV2 to protein changes at the surface that are necessary for kinase activation.

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