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Updated: May 31, 2026

Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange (ABE)
16:33

Detection of Protein Palmitoylation in Cultured Hippocampal Neurons by Immunoprecipitation and Acyl-Biotin Exchange (ABE)

Published on: February 18, 2013

Neurotensin receptor-1 inducible palmitoylation is required for efficient receptor-mediated mitogenic-signaling

Yasser Heakal1, Matthew P Woll, Todd Fox

  • 1The Pennsylvania State University College of Medicine, Hershey, PA USA.

Cancer Biology & Therapy
|July 5, 2011
PubMed

Insights

Neurotensin receptor-1 (NTSR-1) palmitoylation is crucial for its signaling in breast cancer. Inhibiting this process offers a potential therapeutic strategy to block cancer progression by disrupting NTSR-1

Area of Science:

  • Molecular and Cellular Biology
  • Cancer Research
  • Biochemistry

Background:

  • Neurotensin receptor-1 (NTSR-1), a G-protein coupled receptor (GPCR), is implicated in mediating cancer progression.
  • NTSR-1 and its ligand neurotensin (NTS) are co-expressed in breast cancer tissues.
  • Structured membrane microdomains (SMDs) are essential for NTSR-1 mitogenic signaling.

Purpose of the Study:

  • To investigate the role of NTSR-1 palmitoylation in its localization and signaling within SMDs.
  • To determine if inhibiting NTSR-1 palmitoylation can impede breast cancer progression.

Main Methods:

  • Site-directed mutagenesis and pharmacological strategies were used to study NTSR-1 post-translational modifications.
  • Palmitoylation and glycosylation of NTSR-1 were confirmed using various chemical and fluororadiographic methods.
  • Cell viability, apoptosis, and ERK phosphorylation assays assessed the functional consequences of NTSR-1 palmitoylation.

Main Results:

  • NTSR-1 undergoes dual-palmitoylation at Cys381 and Cys383, confirmed in both cancer and overexpression cell models.
  • Inhibition of NTSR-1 palmitoylation reduced NTS-mediated ERK1/2 phosphorylation.
  • Mutations at Cys381 and Cys383 diminished NTSR-1's interaction with Gαq/11 and its localization to SMDs.

Conclusions:

  • Palmitoylation is essential for NTSR-1 localization within SMDs and subsequent signaling.
  • Targeting NTSR-1 palmitoylation presents a novel therapeutic strategy for inhibiting breast cancer progression.

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