Results 41 to 50 of about 38,037 (258)

Parkin-independent mitophagy controls chemotherapeutic response in cancer cells [PDF]

, 2017
Mitophagy is an evolutionarily conserved process that selectively targets impaired mitochondria for degradation. Defects in mitophagy are often associated with diverse pathologies, including cancer.
Bossowski, Jozef P., Chiche, Johanna, Marchetti, Sandrine, Mondragón, Laura, Obba, Sandrine, Proïcs, Emma, Ricci, Jean-Ehrland, Riley, Joel S., Rozier, Romain M., Rubio-Patiño, Camila, Tait, Stephen W.G., Verhoeyen, Els, Villa, Elodie, Zunino, Barbara   +13 more
core   +2 more sources

Depletion of RIPK3 or MLKL blocks TNF-driven necroptosis and switches towards a delayed RIPK1 kinase-dependent apoptosis [PDF]

, 2014
In human cells, the RIPK1-RIPK3-MLKL-PGAM5-Drp1 axis drives tumor necrosis factor (TNF)-induced necroptosis through mitochondrial fission, but whether this pathway is conserved among mammals is not known. To answer this question, we analyzed the presence
Baekelandt, V, Bertrand, Mathieu, Bruggeman, Inge, Dondelinger, Yves, Gonçalves, Amanda, Goossens, Vera, Grootjans, Sasker, Remijsen, Quinten, Roelandt, Ria, Takahashi, Nozomi, Van den Haute, C, Vanden Berghe, Tom, Vandenabeele, Peter, Vanlangenakker, Nele   +13 more
core   +3 more sources

PINK1, cancer and neurodegeneration

Oncoscience, 2016
Cancer and neurodegeneration are two age-related diseases that arise from aberrant signaling in similar cellular systems, those that balance survival and death. Thus, deregulated molecular processes such as DNA damage repair, intracellular energy balance, and key signal transduction systems, including the PI3-kinase/Akt axis can promote tumorigenesis ...
Ciara H, O'Flanagan, Vanessa A, Morais, Cora, O'Neill   +2 more
openaire   +2 more sources

Mitochondrial dynamics–fusion, fission, movement, and mitophagy–in neurodegenerative diseases [PDF]

, 2009
Neurons are metabolically active cells with high energy demands at locations distant from the cell body. As a result, these cells are particularly dependent on mitochondrial function, as reflected by the observation that diseases of mitochondrial ...
Alexander, Baloyannis, Banchs, Bossy-Wetzel, Brockmann, Cassidy-Stone, Chang, Chen, Cho, Clark, D. C. Chan, de Brito, Delettre, Dodson, Exner, Fransson, Frezza, Gispert, H. Chen, Hollenbeck, Kim, Kim, Li, Liot, Lustbader, Macaskill, Meeusen, Milone, Mortiboys, Okamoto, Orr, Park, Parone, Popp, Reis, Suen, Ten Dijke, Trushina, Wang, Waterham, Wood-Kaczmar, Zuchner, Z  chner   +42 more
core   +3 more sources

Sam50 Regulates PINK1-Parkin-Mediated Mitophagy by Controlling PINK1 Stability and Mitochondrial Morphology [PDF]

Cell Reports, 2018
PINK1 and Parkin mediate mitophagy, the cellular process that clears dysfunctional mitochondria. Mitophagy is regulated by mitochondrial dynamics, but the molecules linking these two processes remain poorly understood. Here, we show that Sam50, the core component of the sorting and assembly machinery (SAM), is a critical regulator of mitochondrial ...
Jian, Fenglei, Chen, Dan, Chen, Li, Yan, Chaojun, Lu, Bin, Zhu, Yushan, Chen, Shi, Shi, Anbing, Chan, David C., Song, Zhiyin   +9 more
openaire   +3 more sources

Broad activation of the ubiquitin-proteasome system by Parkin is critical for mitophagy [PDF]

, 2011
Parkin, an E3 ubiquitin ligase implicated in Parkinson's disease, promotes degradation of dysfunctional mitochondria by autophagy. Using proteomic and cellular approaches, we show that upon translocation to mitochondria, Parkin activates the ubiquitin ...
Anh H. Pham, Anna M. Salazar, Chen, Ciechanover, Clark, Cox, David C. Chan, de Godoy, Deng, Deshaies, Ding, Gautier, Gegg, Geisler, Greene, Griparic, Kirkpatrick, Korolchuk, Kuroda, Lee, Matsuda, Michael J. Sweredoski, Narendra, Narendra, Narendra, Narendra, Natalie J. Kolawa, Nickie C. Chan, Okatsu, Ong, Pagliarini, Palacino, Pallanck, Park, Poole, Poole, Rappsilber, Robert L.J. Graham, Shimura, Song, Sonja Hess, Sou, Tai, Tanaka, Twig, Vives-Bauza, Yang, Yao, Ziviani, Ziviani   +49 more
core   +3 more sources

PINK1-dependent phosphorylation of PINK1 and Parkin is essential for mitochondrial quality control [PDF]

Cell Death & Disease, 2016
AbstractMitochondrial dysfunction has been linked to the pathogenesis of a large number of inherited diseases in humans, including Parkinson’s disease, the second most common neurodegenerative disorder. The Parkinson’s disease genes pink1 and parkin, which encode a mitochondrially targeted protein kinase, and an E3 ubiquitin ligase, respectively ...
Zhuang, Na, Li, Lin, Chen, She, Wang, Tao   +3 more
openaire   +2 more sources

The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking [PDF]

Journal of Neurochemistry, 2011
Intramembrane proteolysis is a conserved mechanism that regulates a variety of cellular processes ranging from transcription control to signaling. In mitochondria, the inner membrane rhomboid protease PARL has been implicated in the control of life span and apoptosis by a so far uncharacterized mechanism.
Cathrin Meissner, Holger Lorenz, Andreas Weihofen, Dennis J. Selkoe, Marius K. Lemberg   +4 more
openaire   +3 more sources

Synergistic recruitment of UbcH7~Ub and phosphorylated Ubl domain triggers parkin activation [PDF]

, 2018
The E3 ligase parkin ubiquitinates outer mitochondrial membrane proteins during oxidative stress and is linked to early-onset Parkinson’s disease. Parkin is autoinhibited but is activated by the kinase PINK1 that phosphorylates ubiquitin leading to ...
Aguirre, Jacob D., Barber, Kathryn R., Chaugule, Viduth K., Condos, Tara E.C., Dunkerley, Karen M., Freeman, E Aisha, Konermann, Lars, Shaw, Gary S., Walden, Helen, Xiao, Yiming   +9 more
core   +1 more source

PINK1 phosphorylates ubiquitin predominantly in astrocytes [PDF]

npj Parkinson's Disease, 2019
AbstractLoss-of-function mutations in PINK1 are causally linked to recessively inherited Parkinson’s disease (PD), with marked loss of dopaminergic neurons in the substantia nigra that are required for normal movement. PINK1 is a nuclear-encoded mitochondrial-targeted kinase that phosphorylates a conserved serine at amino acid 65 (pS65) in ubiquitin as
Sandeep K. Barodia, Laura J. McMeekin, Rose B. Creed, Elijah K. Quinones, Rita M. Cowell, Matthew S. Goldberg   +5 more
openaire   +2 more sources