PMID- 24488767
OWN - NLM
STAT- MEDLINE
DCOM- 20150112
LR  - 20211021
IS  - 1460-2083 (Electronic)
IS  - 0964-6906 (Print)
IS  - 0964-6906 (Linking)
VI  - 23
IP  - 12
DP  - 2014 Jun 15
TI  - Fat mass and obesity-associated (FTO) protein interacts with CaMKII and modulates 
      the activity of CREB signaling pathway.
PG  - 3299-306
LID - 10.1093/hmg/ddu043 [doi]
AB  - Polymorphisms in the fat mass and obesity-associated (FTO) gene have been 
      associated with obesity in humans. FTO is a nuclear protein and its physiological 
      function remains largely unknown, but alterations in its expression in mice 
      influence energy expenditure, food intake and, ultimately, body weight. To 
      understand the molecular functions of FTO, we performed a yeast two-hybrid screen 
      to identify the protein(s) that could directly interact with human FTO protein. 
      Using multiple assays, we demonstrate that FTO interacts with three isoforms of 
      calcium/calmodulin-dependent protein kinase II: alpha, beta and gamma, which are protein 
      kinases that phosphorylate a broad range of substrates. This interaction is 
      functional; overexpression of FTO delays the dephosphorylation of cAMP response 
      element-binding protein (CREB) in human neuroblastoma (SK-N-SH) cells, which in 
      turn leads to a dramatic increase in the expression of the CREB targets 
      neuropeptide receptor 1 (NPY1R) and brain-derived neurotrophic factor (BDNF), 
      which already are known to regulate food intake and energy homeostasis. Thus, our 
      results suggest that FTO could modulate obesity by regulating the activity of the 
      CREB signaling pathway.
CI  - (c) The Author 2014. Published by Oxford University Press. All rights reserved. For 
      Permissions, please email: journals.permissions@oup.com.
FAU - Lin, Li
AU  - Lin L
AD  - Department of Human Genetics and.
FAU - Hales, Chadwick M
AU  - Hales CM
AD  - Department of Neurology and Center for Neurodegenerative Diseases, Emory 
      University School of Medicine, Atlanta, GA 30322, USA.
FAU - Garber, Kathryn
AU  - Garber K
AD  - Department of Human Genetics and.
FAU - Jin, Peng
AU  - Jin P
AD  - Department of Human Genetics and peng.jin@emory.edu.
LA  - eng
GR  - R01 MH102690/MH/NIMH NIH HHS/United States
GR  - NS051630/NS/NINDS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20140131
PL  - England
TA  - Hum Mol Genet
JT  - Human molecular genetics
JID - 9208958
RN  - 0 (Brain-Derived Neurotrophic Factor)
RN  - 0 (Proteins)
RN  - 0 (Receptors, Neuropeptide Y)
RN  - 0 (neuropeptide Y-Y1 receptor)
RN  - 1F7A44V6OU (Colforsin)
RN  - 7171WSG8A2 (BDNF protein, human)
RN  - EC 1.14.11.33 (Alpha-Ketoglutarate-Dependent Dioxygenase FTO)
RN  - EC 1.14.11.33 (FTO protein, human)
RN  - EC 2.3.1.48 (CREB-Binding Protein)
RN  - EC 2.3.1.48 (CREBBP protein, human)
RN  - EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinase Type 2)
SB  - IM
MH  - Alpha-Ketoglutarate-Dependent Dioxygenase FTO
MH  - Body Weight/*genetics
MH  - Brain-Derived Neurotrophic Factor/metabolism
MH  - CREB-Binding Protein/*metabolism
MH  - Calcium-Calmodulin-Dependent Protein Kinase Type 2/*metabolism
MH  - Cell Line, Tumor
MH  - Colforsin/pharmacology
MH  - Eating/genetics
MH  - Energy Metabolism
MH  - Gene Expression Regulation
MH  - HEK293 Cells
MH  - Homeostasis
MH  - Humans
MH  - Phosphorylation
MH  - Proteins/*genetics/*metabolism
MH  - Receptors, Neuropeptide Y/metabolism
MH  - *Signal Transduction
PMC - PMC4030783
EDAT- 2014/02/04 06:00
MHDA- 2015/01/13 06:00
PMCR- 2015/06/15
CRDT- 2014/02/04 06:00
PHST- 2014/02/04 06:00 [entrez]
PHST- 2014/02/04 06:00 [pubmed]
PHST- 2015/01/13 06:00 [medline]
PHST- 2015/06/15 00:00 [pmc-release]
AID - ddu043 [pii]
AID - 10.1093/hmg/ddu043 [doi]
PST - ppublish
SO  - Hum Mol Genet. 2014 Jun 15;23(12):3299-306. doi: 10.1093/hmg/ddu043. Epub 2014 
      Jan 31.