A novel ubiquitin-specific protease, synUSP, is localized at the post-synaptic density and post-synaptic lipid raft.

Recent reports suggest an important role for protein ubiquitination in synaptic plasticity. We cloned, from the rat brain, a novel gene that encoded an ubiquitin-specific protease (USP), and termed this protein synaptic ubiquitin-specific protease (synUSP, GenBankTM Accession no. AB073880). The homologous human gene was mapped to a locus on chromosome ...
1p36.12. The deduced synUSP protein consisted of 1036 amino acids, and possessed an ubiquitin-like domain at the C-terminus, Cys- and His-boxes, leucine zipper motifs, and six amino acid-repeats of L/ILCPHG. The protein possessed de-ubiquitinating activity toward a model substrate, as expected from its sequence. The protein of 125 kDa was present in the rat brain; in particular, it was enriched in the post-synaptic density and the dendritic lipid raft fractions. The immunostaining of cortical neurons confirmed the post-synaptic localization. The mRNA for synUSP was localized to dendrites, as well as somas, of neuronal cells. Thus, both the mRNA and the protein were localized in the post-synaptic compartments. These results suggest a regulatory mechanism for the ubiquitin-related system at the post-synaptic sites.
Mesh Terms:
Amino Acid Sequence, Animals, Base Sequence, Brain Chemistry, Cells, Cultured, Cloning, Molecular, Dendrites, Endopeptidases, Membrane Microdomains, Molecular Sequence Data, Mutagenesis, Site-Directed, Neurons, RNA, Messenger, Rats, Rats, Wistar, Sequence Homology, Amino Acid, Subcellular Fractions, Synapses
J. Neurochem.
Date: Nov. 01, 2003
Download Curated Data For This Publication
111357
Switch View:
  • Interactions 2