PMID- 17986859
OWN - NLM
STAT- MEDLINE
DCOM- 20080325
LR  - 20211203
IS  - 1551-4005 (Electronic)
IS  - 1551-4005 (Linking)
VI  - 6
IP  - 22
DP  - 2007 Nov 15
TI  - AMPK/LKB1 signaling in epithelial cell polarity and cell division.
PG  - 2755-9
AB  - Cells must coordinate diverse processes including cell division, cell migration, 
      and cell polarity with the cell's metabolic status. How single molecules 
      coordinate these seemingly distinct cell biological events remains relatively 
      unexplored. AMP-activated protein kinase (AMPK) sits at a unique position as a 
      proposed energy sensor that can interface with diverse signaling molecules 
      ranging from LKB1 to mammalian target of rapamycin (mTOR), affecting processes 
      from ribosomal biogenesis to actin regulation. Determining biologically relevant 
      direct kinase targets remains challenging. Alternatively, one can genetically 
      inactivate a kinase and subsequently characterize cellular and whole animal 
      phenotypes without the kinase's activity. Recent genetic studies inactivating 
      AMPK activity in Drosophila indicate unanticipated roles for AMPK as a regulator 
      of epithelial polarity, consistent with known roles of an upstream activator, 
      LKB1 as a PAR (portioning defective) mutant in Caenorhabditis elegans and 
      polarity regulator. Additional genetic analyses demonstrate that both AMPK and 
      LKB1 function are required for faithful chromosomal segregation during mitosis. 
      At least some of these apparently divergent phenotypes may be mediated through 
      myosin regulatory light chain, and presumably the acto-myosin complex, which can 
      affect both polarity and cell division. Chromosomal integrity defects could also 
      be consistent with LKB1's role as a known human tumor suppressor gene. 
      Elucidating the molecular players that interface with AMPK and their potential 
      energy dependent regulation remains an important challenge to fully understand 
      AMPK signaling.
FAU - Brenman, Jay E
AU  - Brenman JE
AD  - Neuroscience Center, UNC Chapel HillSchool of Medicine, Chapel Hill, North 
      Carolina 27599 USA. brenman@med.unc.edu
LA  - eng
GR  - NIMH 073155/PHS HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20070822
PL  - United States
TA  - Cell Cycle
JT  - Cell cycle (Georgetown, Tex.)
JID - 101137841
RN  - 0 (Multienzyme Complexes)
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
RN  - EC 2.7.11.1 (STK11 protein, human)
RN  - EC 2.7.11.3 (AMP-Activated Protein Kinase Kinases)
RN  - EC 2.7.11.31 (AMP-Activated Protein Kinases)
SB  - IM
MH  - AMP-Activated Protein Kinase Kinases
MH  - AMP-Activated Protein Kinases
MH  - Animals
MH  - Cell Division/*physiology
MH  - Cell Polarity/*physiology
MH  - Epithelial Cells/*cytology/*enzymology/physiology
MH  - Humans
MH  - Multienzyme Complexes/*physiology
MH  - Protein Serine-Threonine Kinases/*physiology
MH  - Signal Transduction/*physiology
RF  - 30
EDAT- 2007/11/08 09:00
MHDA- 2008/03/26 09:00
CRDT- 2007/11/08 09:00
PHST- 2007/11/08 09:00 [pubmed]
PHST- 2008/03/26 09:00 [medline]
PHST- 2007/11/08 09:00 [entrez]
AID - 4927 [pii]
AID - 10.4161/cc.6.22.4927 [doi]
PST - ppublish
SO  - Cell Cycle. 2007 Nov 15;6(22):2755-9. doi: 10.4161/cc.6.22.4927. Epub 2007 Aug 
      22.