PMID- 17827270
OWN - NLM
STAT- MEDLINE
DCOM- 20080114
LR  - 20220408
IS  - 0032-0889 (Print)
IS  - 1532-2548 (Electronic)
IS  - 0032-0889 (Linking)
VI  - 145
IP  - 3
DP  - 2007 Nov
TI  - Phytochrome induces rapid PIF5 phosphorylation and degradation in response to 
      red-light activation.
PG  - 1043-51
AB  - The phytochrome (phy) family of sensory photoreceptors (phyA-phyE in Arabidopsis 
      thaliana) induces changes in target-gene expression upon light-induced 
      translocation to the nucleus, where certain members interact with selected 
      members of the constitutively nuclear basic helix-loop-helix transcription factor 
      family, such as PHYTOCHROME-INTERACTING FACTOR3 (PIF3). Previous evidence 
      indicates that the binding of the photoactivated photoreceptor molecule to PIF3 
      induces rapid phosphorylation of the transcription factor in the cell prior to 
      its degradation via the ubiqitin-proteosome system. To investigate whether this 
      apparent primary signaling mechanism can be generalized to other phy-interacting 
      partners, we have examined the molecular behavior of a second related 
      phy-interacting member of the basic helix-loop-helix family, PIF5, during early 
      deetiolation, immediately following initial exposure of dark-grown seedlings to 
      light. The data show that red light induces very rapid phosphorylation and 
      subsequent degradation (t(1/2) < 5 min) of PIF5 via the proteosome system upon 
      irradiation. Photobiological and genetic evidence indicates that the 
      photoactivated phy molecule acts within 60 s to induce this phosphorylation of 
      PIF5, and that phyA and phyB redundantly dominate this process, with phyD playing 
      an apparently minor role. Collectively, the data support the proposal that the 
      rapid phy-induced phosphorylation of PIF3 and PIF5 may represent the biochemical 
      mechanism of primary signal transfer from photoactivated photoreceptor to binding 
      partner, and that phyA and phyB (and possibly phyD) may signal to multiple, 
      shared partners utilizing this common mechanism.
FAU - Shen, Yu
AU  - Shen Y
AD  - Department of Plant and Microbial Biology, University of California, Berkeley, 
      California 94720, USA.
FAU - Khanna, Rajnish
AU  - Khanna R
FAU - Carle, Christine M
AU  - Carle CM
FAU - Quail, Peter H
AU  - Quail PH
LA  - eng
GR  - GM-47475/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, U.S. Gov't, Non-P.H.S.
DEP - 20070907
PL  - United States
TA  - Plant Physiol
JT  - Plant physiology
JID - 0401224
RN  - 0 (Arabidopsis Proteins)
RN  - 0 (Basic Helix-Loop-Helix Transcription Factors)
RN  - 0 (PHYA protein, Arabidopsis)
RN  - 0 (PHYB protein, Arabidopsis)
RN  - 0 (PIF5 protein, Arabidopsis)
RN  - 0 (Phytochrome A)
RN  - 136250-22-1 (Phytochrome B)
SB  - IM
MH  - Arabidopsis/genetics/*metabolism/*radiation effects
MH  - Arabidopsis Proteins/genetics/*metabolism
MH  - Basic Helix-Loop-Helix Transcription Factors/genetics/*metabolism
MH  - Gene Expression Regulation, Plant/radiation effects
MH  - *Light
MH  - Phosphorylation/radiation effects
MH  - Phytochrome A/genetics/*metabolism
MH  - Phytochrome B/genetics/*metabolism
MH  - Protein Binding
MH  - Protein Denaturation
PMC - PMC2048774
EDAT- 2007/09/11 09:00
MHDA- 2008/01/15 09:00
PMCR- 2007/11/01
CRDT- 2007/09/11 09:00
PHST- 2007/09/11 09:00 [pubmed]
PHST- 2008/01/15 09:00 [medline]
PHST- 2007/09/11 09:00 [entrez]
PHST- 2007/11/01 00:00 [pmc-release]
AID - pp.107.105601 [pii]
AID - 105601 [pii]
AID - 10.1104/pp.107.105601 [doi]
PST - ppublish
SO  - Plant Physiol. 2007 Nov;145(3):1043-51. doi: 10.1104/pp.107.105601. Epub 2007 Sep 
      7.