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

Kazu Kikuchi, Naoto Ishii, Hironobu Asao, Kazuo Sugamura

Research output: Contribution to journalArticlepeer-review

23 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)637-643
Number of pages7
JournalBiochemical and biophysical research communications
Volume306
Issue number3
DOIs
Publication statusPublished - 2003 Jul 4

Keywords

  • AMSH
  • Grb2
  • JAMM motif
  • MPN domain
  • STAMs

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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