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Mechanism of procaspase-8 activation by [c-FLIP.sub.L].(BIOCHEMISTRY)(Author abstract)(Report)

Yu, Jong W. ; Jeffrey, Philip D. ; Shi, Yigong

Proceedings of the National Academy of Sciences of the United States, May 19, 2009, Vol.106(20), p.8169(6) [Tạp chí có phản biện]

ISSN: 0027-8424

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  • Nhan đề:
    Mechanism of procaspase-8 activation by [c-FLIP.sub.L].(BIOCHEMISTRY)(Author abstract)(Report)
  • Tác giả: Yu, Jong W. ; Jeffrey, Philip D. ; Shi, Yigong
  • Chủ đề: Aspartic Proteases -- Properties ; Cell Death -- Research
  • Là 1 phần của: Proceedings of the National Academy of Sciences of the United States, May 19, 2009, Vol.106(20), p.8169(6)
  • Mô tả: Cellular FLICE-inhibitory protein ([c-FLIP.sub.L]) is a key regulator of the extrinsic cell death pathway. Although widely regarded as an inhibitor of initiator caspase activation and cell death, [c-FLIP.sub.L] is also capable of enhancing procaspase-8 activation through heterodimerization of their respective protease domains. However, the underlying mechanism of this activation process remains enigmatic. Here, we demonstrate that cleavage of the intersubunit linker of [c-FLIP.sub.L] by procaspase-8 potentiates the activation process by enhancing heterodimerization between the two proteins and vastly improving the proteolytic activity of unprocessed caspase-(C)8. The crystal structures of the protease-like domain of [c-FLIP.sub.L] alone and in complex with zymogen C8 identify the unique determinants that favor heterodimerization over procaspase-8 homodimerization, and induce the latent active site of zymogen C8 into a productive conformation. Together, these findings provide molecular insights into a key aspect of [c-FLIP.sub.L] function that modulates procaspase-8 activation to elicit diverse responses in different cellular contexts. apoptosis | caspase-8 | extrinsic pathway | cellular FLICE-inhibitory protein
  • Ngôn ngữ: English
  • Số nhận dạng: ISSN: 0027-8424

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