Disease relevance of Snn

• Stannin (Snn), a protein preferentially expressed in TMT-sensitive cells, provides a direct link to the molecular basis for TMT toxicity [1].
• Stannin was absent in the resistant HTB-14 glioma cell line [2].

High impact information on Snn

• In contrast, trimethyltin induced a marked loss of stannin immunoreactivity in hippocampal neurons seven days after injection [3].
• Alterations in hippocampal expression of SNAP-25, GAP-43, stannin and glial fibrillary acidic protein following mechanical and trimethyltin-induced injury in the rat [3].
• Stannin was expressed in several TMT-sensitive cell lines (PC12, T, B cells) and in primary neurons in culture [2].
• The role of stannin in mediating TMT toxicity in primary cultures was investigated by blocking stannin expression with specific antisense oligonucleotides [2].
• Thus, TMT may induce apoptosis in sensitive cells, which is partly mediated by stannin [2].

Biological context of Snn

• Consistent with this, a detailed amino acid sequence analysis shows that Snn contains a putative 14-3-3 protein-binding site located within its hydrophilic loop [1].

Physical interactions of Snn

• The protein stannin binds 14-3-3zeta and modulates mitogen-activated protein kinase signaling [1].

Regulatory relationships of Snn

• In addition, we present the evidence that Snn overexpression results in reduced extracellular regulated kinase activation and increased p38 activation [1].

Other interactions of Snn

• Together, these findings indicate a role of Snn in modulation of MAPK signaling pathways through its interactions with 14-3-3zeta [1].
• In contrast, the activity of c-Jun N-terminal kinase did not change following Snn overexpression [1].

References