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.
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
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
Biochem. Biophys. Res. Commun.
Date: Jul. 04, 2003
PubMed ID: 12810066
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