Palmitoylation of BMPR1a regulates neural stem cell fate

Proc Natl Acad Sci U S A. 2019 Dec 17;116(51):25688-25696. doi: 10.1073/pnas.1912671116. Epub 2019 Nov 26.


Neural stem cells (NSCs) generate neurons and glial cells throughout embryonic and postnatal brain development. The role of S-palmitoylation (also referred to as S-acylation), a reversible posttranslational lipid modification of proteins, in regulating the fate and activity of NSCs remains largely unknown. We used an unbiased screening approach to identify proteins that are S-acylated in mouse NSCs and showed that bone morphogenic protein receptor 1a (BMPR1a), a core mediator of BMP signaling, is palmitoylated. Genetic manipulation of S-acylated sites affects the localization and trafficking of BMPR1a and leads to altered BMP signaling. Strikingly, defective palmitoylation of BMPR1a modulates NSC function within the mouse brain, resulting in enhanced oligodendrogenesis. Thus, we identified a mechanism regulating the behavior of NSCs and provided the framework to characterize dynamic posttranslational lipid modifications of proteins in the context of NSC biology.

Keywords: BMP receptor; neural stem cell; neurogenesis; oligodendrogenesis; palmitoylation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bone Morphogenetic Protein Receptors, Type I* / chemistry
  • Bone Morphogenetic Protein Receptors, Type I* / metabolism
  • Cells, Cultured
  • Lipoylation / physiology*
  • Mice
  • Neural Stem Cells* / chemistry
  • Neural Stem Cells* / cytology
  • Neural Stem Cells* / metabolism
  • Neurogenesis / physiology*


  • Bmpr1a protein, mouse
  • Bone Morphogenetic Protein Receptors, Type I