PMID- 29846113
OWN - NLM
STAT- MEDLINE
DCOM- 20190708
LR  - 20211204
IS  - 1522-1466 (Electronic)
IS  - 1522-1466 (Linking)
VI  - 315
IP  - 3
DP  - 2018 Sep 1
TI  - Mechanistic target of rapamycin: integrating growth factor and nutrient signaling 
      in the collecting duct.
PG  - F413-F416
LID - 10.1152/ajprenal.00170.2018 [doi]
AB  - The renal collecting duct and other postmacula densa sites are the primary 
      tubular regions for fine-tuning of electrolyte homeostasis in the body. A role 
      for the mechanistic target of rapamycin (mTOR), a serine-threonine kinase, has 
      recently been appreciated in this regulation. mTOR exists in two distinct 
      multiprotein functional complexes, i.e., mTORC1 and mTORC2. Upregulation of 
      mTORC1, by growth factors and amino acids, is associated with cell cycle 
      regulation and hypertrophic changes. In contrast, mTORC2 has been demonstrated to 
      have a role in regulating Na(+) and K(+) reabsorptive processes, including those 
      downstream of insulin and serum- and glucocorticoid-regulated kinase (SGK). In 
      addition, mTORC2 can upregulate mTORC1. A number of elegant in vitro and in vivo 
      studies using cell systems and genetically modified mice have revealed mechanisms 
      underlying activation of the epithelial Na(+) channel (ENaC) and the renal outer 
      medullary K(+) channel (ROMK) by mTORC2. Overall, mTOR in its systematic 
      integration of phosphorylative signaling facilitates the delicate balance of 
      whole body electrolyte homeostasis in the face of changes in metabolic status. 
      Thus, inappropriate regulation of renal mTOR has the potential to result in 
      electrolyte disturbances, such as acidosis/alkalosis, hyponatremia, and 
      hypertension. The goal of this minireview is to highlight the physiological role 
      of mTOR in its complexes in regulating electrolyte homeostasis in the 
      aldosterone-sensitive distal nephron.
FAU - Brown, Aaron L
AU  - Brown AL
AD  - Department of Medicine, Georgetown University , Washington, District of Columbia.
FAU - Fluitt, Maurice B
AU  - Fluitt MB
AD  - Department of Medicine, Georgetown University , Washington, District of Columbia.
FAU - Ecelbarger, Carolyn M
AU  - Ecelbarger CM
AD  - Department of Medicine, Georgetown University , Washington, District of Columbia.
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20180530
PL  - United States
TA  - Am J Physiol Renal Physiol
JT  - American journal of physiology. Renal physiology
JID - 100901990
RN  - 0 (Amino Acids)
RN  - 0 (Chlorides)
RN  - 0 (Dietary Proteins)
RN  - 0 (Electrolytes)
RN  - 0 (Intercellular Signaling Peptides and Proteins)
RN  - 9NEZ333N27 (Sodium)
RN  - EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 1)
RN  - EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 2)
RN  - EC 2.7.11.1 (TOR Serine-Threonine Kinases)
RN  - RWP5GA015D (Potassium)
SB  - IM
MH  - Amino Acids/*metabolism
MH  - Animals
MH  - Chlorides/metabolism
MH  - Dietary Proteins/*metabolism
MH  - Electrolytes/*metabolism/urine
MH  - Humans
MH  - Intercellular Signaling Peptides and Proteins/*metabolism
MH  - Kidney Concentrating Ability
MH  - Kidney Tubules, Collecting/*metabolism
MH  - Mechanistic Target of Rapamycin Complex 1/metabolism
MH  - Mechanistic Target of Rapamycin Complex 2/metabolism
MH  - Phosphorylation
MH  - Potassium/metabolism
MH  - Renal Elimination
MH  - Renal Reabsorption
MH  - *Signal Transduction
MH  - Sodium/metabolism
MH  - TOR Serine-Threonine Kinases/genetics/*metabolism
OTO - NOTNLM
OT  - chloride
OT  - insulin
OT  - metabolic syndrome
OT  - potassium
OT  - sodium
EDAT- 2018/05/31 06:00
MHDA- 2019/07/10 06:00
CRDT- 2018/05/31 06:00
PHST- 2018/05/31 06:00 [pubmed]
PHST- 2019/07/10 06:00 [medline]
PHST- 2018/05/31 06:00 [entrez]
AID - 10.1152/ajprenal.00170.2018 [doi]
PST - ppublish
SO  - Am J Physiol Renal Physiol. 2018 Sep 1;315(3):F413-F416. doi: 
      10.1152/ajprenal.00170.2018. Epub 2018 May 30.