Presenilin/gamma-secretase-mediated cleavage of the voltage-gated sodium channel beta2-subunit regulates cell adhesion and migration

J Biol Chem. 2005 Jun 17;280(24):23251-61. doi: 10.1074/jbc.M412938200. Epub 2005 Apr 14.

Abstract

The voltage-gated sodium channel beta2-subunit (beta2) is a member of the IgCAM superfamily and serves as both an adhesion molecule and an auxiliary subunit of the voltage-gated sodium channel. Here we found that beta2 undergoes ectodomain shedding followed by presenilin (PS)-dependent gamma-secretase-mediated cleavage. 12-O-Tetradecanoylphorbol-13-acetate treatment or expression of an alpha-secretase enzyme, ADAM10, resulted in ectodomain cleavage of beta2 in Chinese hamster ovary cells. Subsequent cleavage of the remaining 15-kDa C-terminal fragment (beta2-CTF) was independently inhibited by three specific gamma-secretase inhibitors, expression of the dominant negative form of PS1, and in PS1/PS2 knock-out cells. gamma-Secretase inhibitor treatment also increased endogenous beta2-CTF levels in neuroblastoma cells and mouse primary neuronal cultures. In a cell-free gamma-secretase assay, we detected gamma-secretase activity-dependent generation of a 12 kDa beta2 intracellular domain (ICD), which was loosely associated with the membrane fraction. To assess the functional role of beta2 processing by gamma-secretase, we tested whether N-[N-(3,5-difluorophenylacetyl-l-alanyl)]-S-phenylglycine t-butylester (DAPT), a specific gamma-secretase inhibitor, would alter beta2-mediated cell adhesion and migration. We found that DAPT inhibited cell-cell aggregation and migration in a wound healing assay carried out with Chinese hamster ovary cells expressing beta2. DAPT also reduced migration of neuroblastoma cells in a modified Boyden chamber assay. Since DAPT treatment resulted in increased beta2-CTF levels, we also tested whether beta2-CTFs or beta2-ICDs would directly affect cell migration by overexpressing recombinant proteins. Interestingly, elevated levels of beta2-CTFs, but not ICDs, also blocked cell migration by 81 to 93%. Together, our findings show for the first time that beta2 is a PS/gamma-secretase substrate and gamma-secretase mediated cleavage of beta2-CTF is required for cell-cell adhesion and migration of beta2-expressing cells.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amyloid Precursor Protein Secretases
  • Animals
  • Aspartic Acid Endopeptidases
  • Blotting, Western
  • CHO Cells
  • Cell Adhesion
  • Cell Communication
  • Cell Culture Techniques
  • Cell Membrane / metabolism
  • Cell Movement
  • Cell-Free System
  • Cerebral Cortex / embryology
  • Cricetinae
  • Endopeptidases / biosynthesis
  • Enzyme Inhibitors / pharmacology
  • Humans
  • Membrane Proteins / metabolism*
  • Mice
  • Microscopy, Confocal
  • Molecular Sequence Data
  • Nerve Tissue Proteins
  • Neurons / metabolism
  • Presenilin-1
  • Protein Binding
  • Protein Structure, Tertiary
  • Protein Subunits / chemistry*
  • Protein Subunits / metabolism
  • Recombinant Proteins / chemistry
  • Sequence Homology, Amino Acid
  • Sodium Channels / chemistry*
  • Sodium Channels / metabolism
  • Tetradecanoylphorbol Acetate / chemistry
  • Triglycerides / pharmacology
  • Voltage-Gated Sodium Channel beta-2 Subunit
  • Wound Healing
  • gamma-Aminobutyric Acid / analogs & derivatives*
  • gamma-Aminobutyric Acid / pharmacology

Substances

  • Enzyme Inhibitors
  • Membrane Proteins
  • Nerve Tissue Proteins
  • PSEN1 protein, human
  • Presenilin-1
  • Protein Subunits
  • Recombinant Proteins
  • SCN2B protein, human
  • Sodium Channels
  • Triglycerides
  • Voltage-Gated Sodium Channel beta-2 Subunit
  • gamma-Aminobutyric Acid
  • 1,2-dilinolenoyl-3-(4-aminobutyryl)propane-1,2,3-triol
  • Amyloid Precursor Protein Secretases
  • Endopeptidases
  • Aspartic Acid Endopeptidases
  • BACE1 protein, human
  • Bace1 protein, mouse
  • Tetradecanoylphorbol Acetate