High impact information on Nisch

• The integrin-binding protein Nischarin regulates cell migration by inhibiting PAK [1].
• Conversely, reduction of endogenous levels of Nischarin by RNA interference promotes cell migration [1].
• Rat embryo fibroblasts transfected with Nischarin constructs have "basket-like" networks of peripheral actin filaments, rather than typical stress fibers [2].
• These observations suggest that Nischarin might affect signaling to the cytoskeleton regulated by Rho-family GTPases [2].
• Additionally, suppression of endogenous Nischarin protein with small interfering RNA in PC12 cells enhanced Rac1Q61L and Rac1Q61L-40C activation of NF-kappaB [3].

Biological context of Nisch

• Overexpression of Nischarin markedly reduces alpha5beta1-dependent cell migration in several cell types [2].
• Equally important, the Nischarin ODNs eliminated the production of MAPK(p42/44), a recognized signal transduction product generated by I1-receptor activation in differentiated PC12 cells [4].
• Nischarin and IRAS share the functions of enhancing cell survival, growth and migration [4].
• Bioinformatics modeling indicates that the IRAS and Nischarin may be transmembrane proteins and the convergence information raises the interesting possibility that Nischarin might serve as the I1-receptor [4].

Associations of Nisch with chemical compounds

• Nischarin, a novel intracellular protein, was originally identified as a binding partner for the alpha5beta1 integrin [1].
• To test this hypothesis, we developed antibodies against the Nischarin protein, and conducted signal transduction (functional) studies with the I1-receptor agonist rilmenidine in the presence and absence of Nischarin antisense oligodeoxynucleotides (ODNs) [4].

References