RIPK1 mediates axonal degeneration by promoting inflammation and necroptosis in ALS.

نویسندگان

  • Yasushi Ito
  • Dimitry Ofengeim
  • Ayaz Najafov
  • Sudeshna Das
  • Shahram Saberi
  • Ying Li
  • Junichi Hitomi
  • Hong Zhu
  • Hongbo Chen
  • Lior Mayo
  • Jiefei Geng
  • Palak Amin
  • Judy Park DeWitt
  • Adnan Kasim Mookhtiar
  • Marcus Florez
  • Amanda Tomie Ouchida
  • Jian-bing Fan
  • Manolis Pasparakis
  • Michelle A Kelliher
  • John Ravits
  • Junying Yuan
چکیده

Mutations in the optineurin (OPTN) gene have been implicated in both familial and sporadic amyotrophic lateral sclerosis (ALS). However, the role of this protein in the central nervous system (CNS) and how it may contribute to ALS pathology are unclear. Here, we found that optineurin actively suppressed receptor-interacting kinase 1 (RIPK1)-dependent signaling by regulating its turnover. Loss of OPTN led to progressive dysmyelination and axonal degeneration through engagement of necroptotic machinery in the CNS, including RIPK1, RIPK3, and mixed lineage kinase domain-like protein (MLKL). Furthermore, RIPK1- and RIPK3-mediated axonal pathology was commonly observed in SOD1(G93A) transgenic mice and pathological samples from human ALS patients. Thus, RIPK1 and RIPK3 play a critical role in mediating progressive axonal degeneration. Furthermore, inhibiting RIPK1 kinase may provide an axonal protective strategy for the treatment of ALS and other human degenerative diseases characterized by axonal degeneration.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Axonal Degeneration: RIPK1 Multitasking in ALS

A recent study reports that microglia and oligodendrocytes promote motor neuron degeneration by inducing inflammation and necroptosis in a manner dependent on receptor-interacting kinase 1 (RIPK1). These findings could be significant for our understanding of the neurobiology and treatment of neurodegenerative diseases like amyotrophic lateral sclerosis.

متن کامل

RIPK1 Regulates RIPK3-MLKL-Driven Systemic Inflammation and Emergency Hematopoiesis

Upon ligand binding, RIPK1 is recruited to tumor necrosis factor receptor superfamily (TNFRSF) and Toll-like receptor (TLR) complexes promoting prosurvival and inflammatory signaling. RIPK1 also directly regulates caspase-8-mediated apoptosis or, if caspase-8 activity is blocked, RIPK3-MLKL-dependent necroptosis. We show that C57BL/6 Ripk1(-/-) mice die at birth of systemic inflammation that wa...

متن کامل

SnapShot: Necroptosis

Regulated necrosis, termed necroptosis, is mediated by the kinase activity of RIPK1 and RIPK3. It has distinct cellular features that are different than apoptosis. Necroptosis can be triggered by extracellular stimuli known to activate inflammation and cell death and its intracellular signaling pathway involves necrosome formation and MLKL activation. Inhibition of necroptosis has been shown to...

متن کامل

RIPK1 Blocks Early Postnatal Lethality Mediated by Caspase-8 and RIPK3

Receptor-interacting protein kinase (RIPK)-1 is involved in RIPK3-dependent and -independent signaling pathways leading to cell death and/or inflammation. Genetic ablation of ripk1 causes postnatal lethality, which was not prevented by deletion of ripk3, caspase-8, or fadd. However, animals that lack RIPK1, RIPK3, and either caspase-8 or FADD survived weaning and matured normally. RIPK1 functio...

متن کامل

RIPK1 prevents aberrant ZBP1-initiated necroptosis

Receptor interacting protein kinase 1 (RIPK1) regulates inflammation and cell death, in host defense and homeostasis. The adaptor function of RIPK1 allows pro-survival and inflammatory signaling, while its kinase activity regulates the induction of necroptosis and apoptosis. A new level of regulation through its RIP homotypic interaction motif (RHIM) was recently discovered to suppress necropto...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:
  • Science

دوره 353 6299  شماره 

صفحات  -

تاریخ انتشار 2016