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SNAT2 transceptor signalling via mTOR: a role in cell growth and proliferation?

Jorge Pinilla1, Juan Carlos Aledo, Emma Cwiklinski

  • 1Division of Molecular Physiology, James Black Centre, College of Life Sciences, University of Dundee, Dundee, United Kingdom.

Frontiers in Bioscience (Elite Edition)
|May 31, 2011
PubMed

Insights

Inhibiting amino acid transport via SNAT2 in breast cancer cells reduced proliferation but increased cell size and mTOR signaling. Novel SNAT2-interacting proteins were identified, potentially regulating cell growth.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • MCF-7 human breast cancer cells utilize Na+- and pH-dependent SNAT2 amino acid (AA) transport.
  • SNAT2 plays a crucial role in amino acid uptake and cellular processes.

Purpose of the Study:

  • To investigate the impact of chronic SNAT2 inhibition on MCF-7 breast cancer cell growth and proliferation.
  • To explore the downstream signaling effects and identify proteins interacting with SNAT2.

Main Methods:

  • Cells were incubated with a saturating dose of the non-metabolisable SNAT2 substrate analogue, Me-AIB (10 mM).
  • Cell proliferation, intracellular amino acid concentrations, cell size, and mTOR signaling (p70S6K1 phosphorylation) were analyzed.
  • Proteomic analysis was performed on TAP-tag purified SNAT2 fusion proteins.

Main Results:

  • Chronic Me-AIB incubation reduced cell proliferation by approximately 2-fold and depleted intracellular amino acid pools, including essential branched-chain AAs.
  • Despite reduced amino acid levels, total cellular protein was maintained, and cells showed increased size.
  • Me-AIB elevated mTOR-dependent p70S6K1 phosphorylation, and two novel SNAT2-interacting proteins were identified.

Conclusions:

  • Competitive inhibition of SNAT2 transport affects breast cancer cell proliferation and size.
  • SNAT2 activity influences mTOR signaling pathways, even with depleted intracellular amino acid pools.
  • The identified SNAT2-interacting proteins may regulate signaling pathways involved in protein turnover and cell growth.

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