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Identification of AMSH-LP containing a Jab1/MPN domain metalloenzyme motif.

We have isolated a cDNA clone encoding a new AMSH (associated molecule with the SH3 domain of STAM) family protein, termed AMSH-like protein (AMSH-LP). AMSH-LP has similar characteristics to AMSH; both AMSH-LP and AMSH are expressed ubiquitously in various human tissues, contain a putative nuclear localization signal (NLS), an Mpr/Pad1/N-terminal (MPN) domain, and a Jab1/MPN domain metalloenzyme (JAMM) motif in their structures, and are excluded from the nucleus when lacking either the NLS or MPN domain. Moreover, we observed an enhancement of interleukin 2 (IL-2)-mediated c-myc induction in AMSH-LP-transfected cells similar to that seen in AMSH-transfected cells, suggesting a functional similarity between AMSH-LP and AMSH. However, the present study demonstrated that AMSH-LP, unlike AMSH, fails to bind to the SH3 domains of STAM1 (signal transducing adaptor molecule 1) and Grb2. These results suggest that AMSH-LP and AMSH may have different functions.

Pubmed ID: 12810066

Authors

  • Kikuchi K
  • Ishii N
  • Asao H
  • Sugamura K

Journal

Biochemical and biophysical research communications

Publication Data

July 4, 2003

Associated Grants

None

Mesh Terms

  • Amino Acid Sequence
  • Carrier Proteins
  • Cell Line
  • Cloning, Molecular
  • Endopeptidases
  • Endosomal Sorting Complexes Required for Transport
  • Gene Expression Regulation
  • Genes, myc
  • Humans
  • Molecular Sequence Data
  • Protein Binding
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins
  • Sequence Alignment
  • Tissue Distribution
  • Ubiquitin Thiolesterase
  • src Homology Domains