MLKL: Functions beyond serving as the Executioner of Necroptosis

Recently, necroptosis, as a programmed cell death pathway, has drawn much attention as it has been implicated in multiple pathologies, especially in the field of inflammatory diseases. Pseudokinase mixed lineage kinase domain-like protein (MLKL) serves as a terminal-known obligate effector in the pr...

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Veröffentlicht in:Theranostics Jg. 11; H. 10; S. 4759 - 4769
Hauptverfasser: Zhan, Chaoning, Huang, Minchun, Yang, Xiaojun, Hou, Jin
Format: Journal Article
Sprache:Englisch
Veröffentlicht: Australia Ivyspring International Publisher Pty Ltd 01.01.2021
Ivyspring International Publisher
Schlagworte:
Apoptosis
Heat shock proteins
Homeostasis
Kinases
Lymphoma
Pathogens
Phosphorylation
Plasma
Regulation
Review
Tumor necrosis factor-TNF
inhibitors
therapeutic target
MLKL
structure
necroptosis
ISSN:1838-7640, 1838-7640
Online-Zugang:Volltext
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Zusammenfassung:Recently, necroptosis, as a programmed cell death pathway, has drawn much attention as it has been implicated in multiple pathologies, especially in the field of inflammatory diseases. Pseudokinase mixed lineage kinase domain-like protein (MLKL) serves as a terminal-known obligate effector in the process of necroptosis. To date, the majority of research on MLKL has focused on its role in necroptosis, and the prevailing view has been that the sole function of MLKL is to mediate necroptosis. However, increasing evidence indicates that MLKL can serve as a regulator of many diseases via its non-necroptotic functions. These functions of MLKL shed light on its functional complexity and diversity. In this review, we briefly introduce the current state of knowledge regarding the structure of MLKL, necroptosis signaling, as well as cross-linkages among necroptosis and other regulated cell death pathways, and we particularly highlight recent progress related to newly identified functions and inhibitors of MLKL. These discussions promote a better understanding of the role of MLKL in diseases, which will foster efforts to pharmacologically target this molecule in clinical treatments.
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Competing Interests: The authors have declared that no competing interest exists.
These authors contribute equally to this work.
ISSN:1838-7640
1838-7640
DOI:10.7150/thno.54072