PMID- 26426064
OWN - NLM
STAT- PubMed-not-MEDLINE
DCOM- 20151002
LR  - 20200930
IS  - 2077-0375 (Print)
IS  - 2077-0375 (Electronic)
IS  - 2077-0375 (Linking)
VI  - 5
IP  - 4
DP  - 2015 Sep 29
TI  - Regulation of the Target of Rapamycin and Other Phosphatidylinositol 
      3-Kinase-Related Kinases by Membrane Targeting.
PG  - 553-75
LID - 10.3390/membranes5040553 [doi]
AB  - Phosphatidylinositol 3-kinase-related kinases (PIKKs) play vital roles in the 
      regulation of cell growth, proliferation, survival, and consequently metabolism, 
      as well as in the cellular response to stresses such as ionizing radiation or 
      redox changes. In humans six family members are known to date, namely 
      mammalian/mechanistic target of rapamycin (mTOR), ataxia-telangiectasia mutated 
      (ATM), ataxia- and Rad3-related (ATR), DNA-dependent protein kinase catalytic 
      subunit (DNA-PKcs), suppressor of morphogenesis in genitalia-1 (SMG-1), and 
      transformation/transcription domain-associated protein (TRRAP). All fulfill 
      rather diverse functions and most of them have been detected in different 
      cellular compartments including various cellular membranes. It has been suggested 
      that the regulation of the localization of signaling proteins allows for 
      generating a locally specific output. Moreover, spatial partitioning is expected 
      to improve the reliability of biochemical signaling. Since these assumptions may 
      also be true for the regulation of PIKK function, the current knowledge about the 
      regulation of the localization of PIKKs at different cellular (membrane) 
      compartments by a network of interactions is reviewed. Membrane targeting can 
      involve direct lipid-/membrane interactions as well as interactions with 
      membrane-anchored regulatory proteins, such as, for example, small GTPases, or a 
      combination of both.
FAU - De Cicco, Maristella
AU  - De Cicco M
AD  - Department of Chemistry, Biomolecular NMR Spectroscopy, Technische Universitat 
      Munchen, Lichtenbergstr. 4, Garching 85747, Germany. m.de-cicco@tum.de.
FAU - Rahim, Munirah S Abd
AU  - Rahim MS
AD  - Department of Chemistry, Biomolecular NMR Spectroscopy, Technische Universitat 
      Munchen, Lichtenbergstr. 4, Garching 85747, Germany. munirah.rahim@tum.de.
FAU - Dames, Sonja A
AU  - Dames SA
AD  - Department of Chemistry, Biomolecular NMR Spectroscopy, Technische Universitat 
      Munchen, Lichtenbergstr. 4, Garching 85747, Germany. sonja.dames@tum.de.
AD  - Institute of Structural Biology, Helmholtz Zentrum Munchen, Ingolstadter Landstr. 
      1, Neuherberg 85764, Germany. sonja.dames@tum.de.
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20150929
PL  - Switzerland
TA  - Membranes (Basel)
JT  - Membranes
JID - 101577807
PMC - PMC4703999
OTO - NOTNLM
OT  - ATM
OT  - ATR
OT  - DNA-PKcs
OT  - SMG-1
OT  - TRRAP
OT  - mTOR
OT  - membrane targeting
OT  - phosphatidylinositol-3 kinase-related kinase
OT  - protein-membrane interaction
OT  - signal transduction
EDAT- 2015/10/02 06:00
MHDA- 2015/10/02 06:01
PMCR- 2015/12/01
CRDT- 2015/10/02 06:00
PHST- 2015/08/26 00:00 [received]
PHST- 2015/09/24 00:00 [accepted]
PHST- 2015/10/02 06:00 [entrez]
PHST- 2015/10/02 06:00 [pubmed]
PHST- 2015/10/02 06:01 [medline]
PHST- 2015/12/01 00:00 [pmc-release]
AID - membranes5040553 [pii]
AID - membranes-05-00553 [pii]
AID - 10.3390/membranes5040553 [doi]
PST - epublish
SO  - Membranes (Basel). 2015 Sep 29;5(4):553-75. doi: 10.3390/membranes5040553.