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The mammalian target of rapamycin  (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1  (mTORC1) and mTOR complex 2  (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast,  mTORC2 consists of a...
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Insulin-regulated protein palmitoylation impacts endothelial cell function.

Xiaochao Wei1, Haowei Song, Clay F Semenkovich

  • 1From the Division of Endocrinology, Metabolism, and Lipid Research (X.W., H.S., C.F.S.) and Department of Cell Biology and Physiology (C.F.S.), Washington University School of Medicine, St. Louis, MO.

Arteriosclerosis, Thrombosis, and Vascular Biology
|December 21, 2013
PubMed
Summary

Insulin signaling impacts endothelial cell function by altering protein palmitoylation, a key post-translational modification. This study identifies novel insulin-regulated palmitoylated proteins, including PAFAH1b3, crucial for angiogenesis and cell migration in vascular health.

Keywords:
endothelial cellsinsulinlipoylation

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Area of Science:

  • Endocrinology and Metabolism
  • Cell Biology
  • Proteomics

Background:

  • Insulin signaling defects are linked to endothelial dysfunction and cardiovascular disease.
  • The role of insulin in regulating protein S-palmitoylation, a critical post-translational modification, within endothelial cells is largely unknown.
  • Understanding these mechanisms is vital for addressing vascular complications.

Purpose of the Study:

  • To investigate whether insulin modulates protein palmitoylation in human endothelial cells.
  • To identify novel insulin-regulated palmitoylated proteins and their role in endothelial cell function.
  • To explore the impact of palmitoylation on insulin-induced angiogenesis and cell migration.

Main Methods:

  • Quantitative proteomic profiling using acyl-biotin exchange chemistry and stable isotope labeling.
  • Identification of palmitoylated proteins and assessment of insulin-induced changes.
  • Functional assays including in vitro angiogenesis, cell migration, and protein-specific mutagenesis.

Main Results:

  • Identified approximately 380 putative palmitoylated proteins, with over 200 previously unknown.
  • Approximately 10% of these proteins showed altered palmitoylation in response to insulin.
  • Insulin stimulated palmitoylation of PAFAH1b3, a protein critical for angiogenesis and cell migration, without altering its abundance.
  • Inhibition of palmitoylation or PAFAH1b3 knockdown impaired insulin-induced angiogenesis and cell migration.

Conclusions:

  • Protein S-palmitoylation is a novel target of insulin signaling in endothelial cells.
  • PAFAH1b3 is a newly identified insulin-regulated palmitoylated protein essential for endothelial cell migration and angiogenesis.
  • Proteomics offers a powerful approach to discover insulin-inducible palmitoylation targets relevant to vascular health.