PMID- 20434335
OWN - NLM
STAT- MEDLINE
DCOM- 20100830
LR  - 20220129
IS  - 1879-0445 (Electronic)
IS  - 0960-9822 (Print)
IS  - 0960-9822 (Linking)
VI  - 20
IP  - 9
DP  - 2010 May 11
TI  - Modulation of fat:dachsous binding by the cadherin domain kinase four-jointed.
PG  - 811-7
LID - 10.1016/j.cub.2010.04.016 [doi]
AB  - In addition to quantitative differences in morphogen signaling specifying cell 
      fates, the vector and slope of morphogen gradients influence planar cell polarity 
      (PCP) and growth. The cadherin Fat plays a central role in this process. Fat 
      regulates PCP and growth through distinct downstream pathways, each involving the 
      establishment of molecular polarity within cells. Fat is regulated by the 
      cadherin Dachsous (Ds) and the protein kinase Four-jointed (Fj), which are 
      expressed in gradients in many tissues. Previous studies have implied that Fat is 
      regulated by the vector and slope of these expression gradients. Here, we 
      characterize how cells interpret the Fj gradient. We demonstrate that Fj both 
      promotes the ability of Fat to bind to its ligand Ds and inhibits the ability of 
      Ds to bind Fat. Consequently, the juxtaposition of cells with differing Fj 
      expression results in asymmetric Fat:Ds binding. We also show that the influence 
      of Fj on Fat is a direct consequence of Fat phosphorylation and identify a 
      phosphorylation site important for the stimulation of Fat:Ds binding by Fj. Our 
      results define a molecular mechanism by which a morphogen gradient can drive the 
      polarization of Fat activity to influence PCP and growth.
CI  - (c) 2010 Elsevier Ltd. All rights reserved.
FAU - Simon, Michael A
AU  - Simon MA
AD  - Department of Biology, Stanford University, Stanford, CA 94305, USA. 
      msimon@stanford.edu
FAU - Xu, Aiguo
AU  - Xu A
FAU - Ishikawa, Hiroyuki O
AU  - Ishikawa HO
FAU - Irvine, Kenneth D
AU  - Irvine KD
LA  - eng
GR  - GM069923/GM/NIGMS NIH HHS/United States
GR  - R01 GM078620/GM/NIGMS NIH HHS/United States
GR  - GM078620/GM/NIGMS NIH HHS/United States
GR  - R01 GM069923/GM/NIGMS NIH HHS/United States
GR  - R01 GM069923-04/GM/NIGMS NIH HHS/United States
GR  - HHMI/Howard Hughes Medical Institute/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20100429
PL  - England
TA  - Curr Biol
JT  - Current biology : CB
JID - 9107782
RN  - 0 (Cadherins)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Drosophila Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (ds protein, Drosophila)
RN  - 0 (fj protein, Drosophila)
RN  - 0 (ft protein, Drosophila)
SB  - IM
MH  - Animals
MH  - Binding Sites/genetics/physiology
MH  - Cadherins/genetics/*physiology
MH  - Cell Adhesion Molecules/genetics/*physiology
MH  - Cell Line
MH  - Cell Polarity/genetics/physiology
MH  - Drosophila Proteins/genetics/*physiology
MH  - Drosophila melanogaster/genetics/*growth & development
MH  - Gene Expression Regulation, Developmental/genetics/physiology
MH  - Genes, Developmental/genetics/physiology
MH  - Membrane Glycoproteins/genetics/*physiology
MH  - Phosphorylation
PMC - PMC2884055
MID - NIHMS206905
EDAT- 2010/05/04 06:00
MHDA- 2010/08/31 06:00
PMCR- 2010/11/11
CRDT- 2010/05/04 06:00
PHST- 2010/01/23 00:00 [received]
PHST- 2010/03/25 00:00 [revised]
PHST- 2010/04/12 00:00 [accepted]
PHST- 2010/05/04 06:00 [entrez]
PHST- 2010/05/04 06:00 [pubmed]
PHST- 2010/08/31 06:00 [medline]
PHST- 2010/11/11 00:00 [pmc-release]
AID - S0960-9822(10)00452-5 [pii]
AID - 10.1016/j.cub.2010.04.016 [doi]
PST - ppublish
SO  - Curr Biol. 2010 May 11;20(9):811-7. doi: 10.1016/j.cub.2010.04.016. Epub 2010 Apr 
      29.