tailieunhanh - Báo cáo khoa học: Subcellular compartmentalization of FADD as a new level of regulation in death receptor signaling

Fas-associated protein with death domain (FADD) is an essential adaptor protein in death receptor-mediated signal transduction. During apoptotic signaling, FADD functions in the cytoplasm, where it couples activated receptors with initiator caspase-8. However, in resting cells, FADD is pre-dominantly stored in the nucleus. In this study, we examined the modalities of FADD intracellular trafficking. | ễFEBS Journal Subcellular compartmentalization of FADD as a new level of regulation in death receptor signaling Niko Foger1 Silvia Bulfone-Paus1 Andrew C. Chan2 and Kyeong-Hee Lee1 1 Department of Immunology and CellBiology Research Center Borstel Leibniz Center for Medicine and Biosciences Germany 2 Department of Immunology Genentech Inc. San Francisco CA USA Keywords apoptosis CD95 compartmentalization FADD nuclear trafficking Correspondence . Lee Department of Immunology and CellBiology Research Center Borstel Leibniz Center for Medicine and Biosciences Parkallee 22 23845 Borstel Germany Fax 49 4537 1884904 Tel 49 4537 188585 E-mail klee@ Received 30 April 2009 accepted 4 June 2009 doi Fas-associated protein with death domain FADD is an essential adaptor protein in death receptor-mediated signal transduction. During apoptotic signaling FADD functions in the cytoplasm where it couples activated receptors with initiator caspase-8. However in resting cells FADD is predominantly stored in the nucleus. In this study we examined the modalities of FADD intracellular trafficking. We demonstrate that upon CD95 activation FADD redistributes from the nucleus to the cytoplasm. This inducible nuclear-cytoplasmic translocation of FADD is independent of CD95 internalization formation of the death-inducing signaling complex and caspase-8 activation. In contrast to nuclear export of FADD its subsequent recruitment and accumulation at endosomes containing internalized CD95 requires a caspase-8-dependent feedback loop. These data indicate the existence of differential pathways directing FADD nuclear export and cytoplasmic trafficking and identify subcellular compartmentalization of FADD as a novel regulatory mechanism in death receptor signaling. Introduction CD95 Fas Apo-1 TNFRSF6 is a prototypic death receptor belonging to the tumor necrosis factor receptor superfamily. CD95 is expressed on the surface of cells as preassociated .

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