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Revealing eEF-2 kinase: recent structural insights into function
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DOI：10.1016/j.tibs.2023.11.004.png)
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摘要
En 中文
The alpha-kinase eukaryotic elongation factor 2 kinase (eEF-2K) regulates translational elongation by phosphorylating its ribosome-associated substrate, the GTPase eEF-2. eEF-2K is activated by calmodulin (CaM) through a distinctive mechanism unlike that in other CaM-dependent kinases (CAMK). We describe recent structural insights into this unique activation process and examine the effects of specific regulatory signals on this mechanism. We also highlight key unanswered questions to guide future structure-function studies. These include structural mechanisms which enable eEF-2K to interact with upstream/downstream partners and facilitate its integration of diverse inputs, including Ca2+ transients, phosphorylation mediated by energy/nutrient-sensing pathways, pH changes, and metabolites. Answering these questions is key to establishing how eEF-2K harmonizes translation with cellular requirements within the boundaries of its molecular landscape.
Keyword:
ELONGATION FACTOR-2 KINASE
PROTEIN-KINASES
FACTOR-II
MOLECULAR-MECHANISM
CATALYTIC DOMAIN
ALPHA-KINASES
PHOSPHORYLATION
ACTIVATION
CALMODULIN
SUBSTRATE
期刊
IF:
11
论文数:
6.6K
被引数:
2.0W
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引用论文
Dynamics connect substrate recognition to catalysis in protein kinase A.png)
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