GABA(A) receptor cell surface number and subunit stability are regulated by the ubiquitin-like protein Plic-1

Nat Neurosci. 2001 Sep;4(9):908-16. doi: 10.1038/nn0901-908.


Controlling the number of functional gamma-aminobutyric acid A (GABA(A)) receptors in neuronal membranes is a crucial factor for the efficacy of inhibitory neurotransmission. Here we describe the direct interaction of GABA(A) receptors with the ubiquitin-like protein Plic-1. Furthermore, Plic-1 is enriched at inhibitory synapses and is associated with subsynaptic membranes. Functionally, Plic-1 facilitates GABA(A) receptor cell surface expression without affecting the rate of receptor internalization. Plic-1 also enhances the stability of intracellular GABA(A) receptor subunits, increasing the number of receptors available for insertion into the plasma membrane. Our study identifies a previously unknown role for Plic-1, a modulation of GABA(A) receptor cell surface number, which suggests that Plic-1 facilitates accumulation of these receptors in dendritic membranes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • Autophagy-Related Proteins
  • Carrier Proteins*
  • Cell Cycle Proteins*
  • Cell Membrane / metabolism
  • Drug Stability
  • Protein Isoforms / metabolism
  • Rats
  • Receptors, GABA-A / metabolism*
  • Subcellular Fractions / metabolism
  • Tissue Distribution
  • Ubiquitins / metabolism
  • Ubiquitins / physiology*


  • Adaptor Proteins, Signal Transducing
  • Autophagy-Related Proteins
  • Carrier Proteins
  • Cell Cycle Proteins
  • Protein Isoforms
  • Receptors, GABA-A
  • UBQLN1 protein, human
  • Ubiquitins