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Molecular & Cellular Oncology Volume 7, 2020 - Issue 5
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HSP70 promotes MLKL polymerization and necroptosis

Andrea N. Johnstona Department of Veterinary Clinical Sciences, School of Veterinary Medicine, Louisiana State University, Baton Rouge, LA, USA;b Department of Molecular Biology, The University of Texas Southwestern Medical Center, Dallas, TX, USAORCID Iconhttps://orcid.org/0000-0003-1082-1155View further author information
ORCID Icon &
Zhigao Wangb Department of Molecular Biology, The University of Texas Southwestern Medical Center, Dallas, TX, USACorrespondence[email protected]
ORCID Iconhttps://orcid.org/0000-0002-6544-4302View further author information
ORCID Icon
Article: 1791561 | Received 24 Jun 2020, Accepted 29 Jun 2020, Published online: 14 Jul 2020

References

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  • Liu S, Liu H, Johnston A, Hanna-Addams S, Reynoso E, Xiang Y, Wang Z. MLKL forms disulfide bond-dependent amyloid-like polymers to induce necroptosis. Proc Natl Acad Sci U S A. 2017;114:E7450–E7459. doi:10.1073/pnas.1707531114.
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  • Jacobsen AV, Lowes KN, Tanzer MC, Lucet IS, Hildebrand JM, Petrie EJ, van Delft MF, Liu Z, Conos SA, Zhang J-G, et al. HSP90 activity is required for MLKL oligomerisation and membrane translocation and the induction of necroptotic cell death. Cell Death Dis. 2016;7:e2051. doi:10.1038/cddis.2015.386.
  • Srinivasan SR, Cesa LC, Li X, Julien O, Zhuang M, Shao H, Chung J, Maillard I, Wells JA, Duckett CS, et al. Heat shock protein 70 (Hsp70) suppresses RIP1-dependent apoptotic and necroptotic cascades. Mol Cancer Res. 2018;16:58–68. doi:10.1158/1541-7786.MCR-17-0408.

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