eEF2K as an important kinase associated with cancer survival and prognosis.

Autor: Wang N; The Second Surgical Department of Breast Cancer, Tianjin Medical University Cancer Institute & Hospital, National Clinical Research Center for Cancer, Key Laboratory of Cancer Prevention and Therapy, Tianjin, 30071, China.; School of Medicine, Nankai University, Tianjin, 300071, China.; Department of Cancer Biology, Wake Forest University School of Medicine, Atrium Health Wake Forest Baptist Comprehensive Cancer Center, Winston-Salem, NC, USA., Cen LL; Key laboratory of molecular pathology in Tumors of Guangxi Higher Education Institutions, Department of Pathology, the Affiliated Hospital of Youjiang Medical University for Nationalities, Baise City, 533000, Guangxi Zhuang Autonomous Region, China.; Guangxi Academy of Medical Sciences, Department of Infectious Disease, The People's Hospital of Guangxi Zhuang Autonomous Region, Nanning, 530021, China., Tian Z; Youjiang Medical University for Nationalities, Baise City, 533000, Guangxi Zhuang Autonomous Region, China., An MM; Key laboratory of molecular pathology in Tumors of Guangxi Higher Education Institutions, Department of Pathology, the Affiliated Hospital of Youjiang Medical University for Nationalities, Baise City, 533000, Guangxi Zhuang Autonomous Region, China., Gu Q; Key laboratory of molecular pathology in Tumors of Guangxi Higher Education Institutions, Department of Pathology, the Affiliated Hospital of Youjiang Medical University for Nationalities, Baise City, 533000, Guangxi Zhuang Autonomous Region, China., Zhou XH; Key laboratory of molecular pathology in Tumors of Guangxi Higher Education Institutions, Department of Pathology, the Affiliated Hospital of Youjiang Medical University for Nationalities, Baise City, 533000, Guangxi Zhuang Autonomous Region, China., Zhang YH; Key laboratory of molecular pathology in Tumors of Guangxi Higher Education Institutions, Department of Pathology, the Affiliated Hospital of Youjiang Medical University for Nationalities, Baise City, 533000, Guangxi Zhuang Autonomous Region, China., Liu L; Atkins Academic & Technology High School, Winston-Salem, NC, 27101, USA., Zhang J; Department of Neurosurgery, Peking University International Hospital, Beijing, 102206, China., Yang D; Key laboratory of molecular pathology in Tumors of Guangxi Higher Education Institutions, Department of Pathology, the Affiliated Hospital of Youjiang Medical University for Nationalities, Baise City, 533000, Guangxi Zhuang Autonomous Region, China., Huang YZ; Key laboratory of molecular pathology in Tumors of Guangxi Higher Education Institutions, Department of Pathology, the Affiliated Hospital of Youjiang Medical University for Nationalities, Baise City, 533000, Guangxi Zhuang Autonomous Region, China., Long XD; Key laboratory of molecular pathology in Tumors of Guangxi Higher Education Institutions, Department of Pathology, the Affiliated Hospital of Youjiang Medical University for Nationalities, Baise City, 533000, Guangxi Zhuang Autonomous Region, China. longxidai@163.com., Yang Q; Key laboratory of molecular pathology in Tumors of Guangxi Higher Education Institutions, Department of Pathology, the Affiliated Hospital of Youjiang Medical University for Nationalities, Baise City, 533000, Guangxi Zhuang Autonomous Region, China. yangqian@ymun.edu.cn.
Jazyk: angličtina
Zdroj: Scientific reports [Sci Rep] 2024 Nov 26; Vol. 14 (1), pp. 29284. Date of Electronic Publication: 2024 Nov 26.
DOI: 10.1038/s41598-024-78652-4
Abstrakt: Eukaryotic Elongation Factor 2 Kinase (eEF2K), a member of the α-kinase family, services as a crucial negative regulator of protein synthesis, particularly under conditions of cellular stress. A pan-cancer analysis of eEF2K expression, genetic variants, and clinical relevance across multiple tumor types was performed using data from the Cancer Genome Atlas (TCGA) and GEO. Our findings suggest that eEF2K has dual roles in cancer progression, with its expression correlating with patient prognosis. Significant phosphorylation of eEF2 at T57, Y434, and T59 was observed, which may regulate protein synthesis during stress. The elevated T59 phosphorylation in COAD, despite the low eEF2K expression, indicates that this may be regulated by alternative kinases, such as AMPK or mTOR. This suggests that compensatory mechanisms may be involved. In addition to modulating eEF2 phosphorylation, eEF2K is involved in a number of other processes, including peptidyl-serine phosphorylation, the G2/M transition, and the MAPK cascade. The protein products of eEF2K are capable of localizing to the nucleus, cytoplasm, and cytosol, where they bind to a range of proteins, including ATP and calcium ions. These findings provide novel insights into the role of eEF2K in cancer biology and suggest that the targeting of eEF2K and eEF2 phosphorylation may offer promising therapeutic strategies.
Competing Interests: Declarations. Competing interests: The authors declare no competing interests.
(© 2024. The Author(s).)
Databáze: MEDLINE
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