Ectodermal Dysplasia
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Data from S. Rahighi et al provide new insights into cell biology
2009 MAY 26 - (NewsRx.com) -- According to a study from Tsukuba, Japan, "Activation of nuclear factor-kappa B (NF-kappa B), a key mediator of inducible transcription in immunity, requires binding of NF-kappa B essential modulator (NEMO) to ubiquitinated substrates. Here, we report that the UBAN (ubiquitin binding in ABIN and NEMO) motif of NEMO selectively binds linear (head-to-tail) ubiquitin chains." "Crystal structures of the UBAN motif revealed a parallel coiled-coil dimer that formed a heterotetrameric complex with two linear diubiquitin molecules. The UBAN dimer contacted all four ubiquitin moieties, and the integrity of each binding site was required for efficient NF-kappa B activation. Binding occurred via a surface on the proximal ubiquitin moiety and the canonical Ile44 surface on the distal one, thereby providing specificity for linear chain recognition," wrote S. Rahighi and colleagues. The researchers concluded: "Residues of NEMO involved in binding linear ubiquitin chains are required for NF-kappa B activation by TNF-alpha and other agonists, providing an explanation for the detrimental effect of NEMO mutations in patients suffering from X-linked ectodermal dysplasia and immunodeficiency." Rahighi and colleagues published the results of their research in Cell (Specific Recognition of Linear Ubiquitin Chains by NEMO Is Important for NF-kappa B Activation. Cell, 2009;136(6):1098-1109). For additional information, contact S. Wakatsuki, High Energy Accelerator Research Organization KEK, Structural Biology Research Center, Photon Factory, Institute Materials Structural Science, Tsukuba, Ibaraki 3050801, Japan. The publisher of the journal Cell can be contacted at: Cell Press, 600 Technology Square, 5TH Floor, Cambridge, MA 02139, USA. Keywords: Japan, Tsukuba, Life Sciences, Cell Biology. This article was prepared by Science Letter editors from staff and other reports. Copyright 2009, Science Letter via NewsRx.com.
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