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Gene Review

STAMBP  -  STAM binding protein

Homo sapiens

Synonyms: AMSH, Associated molecule with the SH3 domain of STAM, Endosome-associated ubiquitin isopeptidase, MICCAP, STAM-binding protein
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Disease relevance of STAMBP

  • The potential functions of RNF11-mediated degradation of AMSH in breast cancer are discussed [1].
  • We also show that a catalytically inactive AMSH inhibits retroviral budding in a dominant-negative manner and induces the accumulation of ubiquitinated forms of an endosomal cargo, namely murine leukemia virus Gag [2].

High impact information on STAMBP

  • Two deubiquitinating enzymes, AMSH and UBPY, interact with ESCRT protein components but exert opposite effects upon the rate of epidermal growth factor receptor downregulation [3].
  • An inactivating mutation (D348A) in AMSH leads to accumulation of ubiquitin on endosomes and the concomitant stabilization of a ubiquitinated form of STAM, which requires an intact ubiquitin interaction motif (UIM) within STAM [4].
  • We propose that AMSH is a deubiquitinating enzyme with functions at the endosome, which oppose the ubiquitin-dependent sorting of receptors to lysosomes [4].
  • Loss of neurons in the hippocampus and cerebral cortex of AMSH-deficient mice [5].
  • Furthermore, AMSH-deficient hippocampal neuronal cells were unable to survive in vitro, even in the presence of several stimulatory cytokines, while AMSH-deficient cerebellar neurons, thymocytes, and embryonic fibroblasts survived normally [5].

Biological context of STAMBP


Anatomical context of STAMBP

  • AMSH mutant deleted of the C-terminal half conferred dominant negative effects on signaling for DNA synthesis and c-myc induction mediated by interleukin 2 and granulocyte macrophage-colony-stimulating factor [6].

Associations of STAMBP with chemical compounds

  • However, all the AMSH-deficient mice exhibited postnatal growth retardation and died between postnatal day 19 (P19) and P23 [5].
  • Targeting of AMSH to Endosomes Is Required for Epidermal Growth Factor Receptor Degradation [8].

Physical interactions of STAMBP

  • Here, we show that RNF11 binds to AMSH in mammalian cells and that this interaction is independent of the RNF11 RING-finger domain and the PY motif [1].
  • In contrast, a mutant of AMSH that lacks the ability to bind STAM localized normally on endosomes [9].

Regulatory relationships of STAMBP

  • CONCLUSIONS: This report implicates AMSH and AMSH-2 as a novel family of molecules that positively regulate the TGF-beta signaling pathway [10].

Other interactions of STAMBP

  • We have looked for similar activity in associated molecule with the SH3 domain of STAM (AMSH), a JAMM domain-containing protein that associates with the SH3-domain of STAM, a protein, which regulates receptor sorting at the endosome [4].
  • These results suggest that AMSH-LP and AMSH may have different functions [11].
  • These results suggest that AMSH plays a critical role in the cytokine-mediated intracellular signal transduction downstream of the Jak2/Jak3.STAM complex [6].
  • However, deletion of the clathrin-binding site from the proteins, as well as RNA interference-mediated depletion of clathrin heavy chain, resulted in a failure of AMSH and AMSH-LP to localize on endosomes [9].
  • In particular, we show that two further MIT domain-containing proteins (AMSH/STAMBP and LOC129531) interact with multiple components of the human ESCRT III complex [12].

Analytical, diagnostic and therapeutic context of STAMBP


  1. An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein. Li, H., Seth, A. Oncogene (2004) [Pubmed]
  2. Interaction of AMSH with ESCRT-III and deubiquitination of endosomal cargo. Agromayor, M., Martin-Serrano, J. J. Biol. Chem. (2006) [Pubmed]
  3. Endocytosis: the DUB version. Clague, M.J., Urb??, S. Trends Cell Biol. (2006) [Pubmed]
  4. AMSH is an endosome-associated ubiquitin isopeptidase. McCullough, J., Clague, M.J., Urbé, S. J. Cell Biol. (2004) [Pubmed]
  5. Loss of neurons in the hippocampus and cerebral cortex of AMSH-deficient mice. Ishii, N., Owada, Y., Yamada, M., Miura, S., Murata, K., Asao, H., Kondo, H., Sugamura, K. Mol. Cell. Biol. (2001) [Pubmed]
  6. Possible involvement of a novel STAM-associated molecule "AMSH" in intracellular signal transduction mediated by cytokines. Tanaka, N., Kaneko, K., Asao, H., Kasai, H., Endo, Y., Fujita, T., Takeshita, T., Sugamura, K. J. Biol. Chem. (1999) [Pubmed]
  7. Phosphorylation of the proline-rich domain of Xp95 modulates Xp95 interaction with partner proteins. Dejournett, R.E., Kobayashi, R., Pan, S., Wu, C., Etkin, L.D., Clark, R.B., B??gler, O., Kuang, J. Biochem. J. (2007) [Pubmed]
  8. Targeting of AMSH to Endosomes Is Required for Epidermal Growth Factor Receptor Degradation. Ma, Y.M., Boucrot, E., Villén, J., Affar, e.l. .B., Gygi, S.P., Göttlinger, H.G., Kirchhausen, T. J. Biol. Chem. (2007) [Pubmed]
  9. Clathrin anchors deubiquitinating enzymes, AMSH and AMSH-like protein, on early endosomes. Nakamura, M., Tanaka, N., Kitamura, N., Komada, M. Genes Cells (2006) [Pubmed]
  10. Cloning of a novel signaling molecule, AMSH-2, that potentiates transforming growth factor beta signaling. Ibarrola, N., Kratchmarova, I., Nakajima, D., Schiemann, W.P., Moustakas, A., Pandey, A., Mann, M. BMC Cell Biol. (2004) [Pubmed]
  11. Identification of AMSH-LP containing a Jab1/MPN domain metalloenzyme motif. Kikuchi, K., Ishii, N., Asao, H., Sugamura, K. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  12. A systematic analysis of human CHMP protein interactions: Additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex. Tsang, H.T., Connell, J.W., Brown, S.E., Thompson, A., Reid, E., Sanderson, C.M. Genomics (2006) [Pubmed]
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