The F-box proteins (FBPs) in esophageal tumorigenesis are pivotal as they govern a broad array of basic physiological responses including cell growth, cell death and DNA damage repair. Esophageal cancer (EC) is a common and highly aggressive cancer worldwide. Aberrant stabilization of crucial proteins participates in esophageal tumorigenesis. Recently, growing evidence has shown that FBPs play a critical role in oncogenesis, invasion, metastasis and prognosis assessment of EC. In this review we summarized published data on the roles of known FBPs, their respective substrates and the key signaling pathways, in the development of EC, aiming to uncover new ways for the rational design of targeted therapies in EC.
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http://dx.doi.org/10.3892/ijo.2016.3325 | DOI Listing |
Nat Commun
January 2025
School of Life Sciences, BK21 FOUR KNU Creative BioRearch Group, Kyungpook National University, Daegu, South Korea.
Lysophagy eliminates damaged lysosomes and is crucial to cellular homeostasis; however, its underlying mechanisms are not entirely understood. We screen a ubiquitination-related compound library and determine that the substrate recognition component of the SCF-type E3 ubiquitin ligase complex, SCF(FBXO3), which is a critical lysophagy regulator. Inhibition of FBXO3 reduces lysophagy and lysophagic flux in response to L-leucyl-L-leucine methyl ester (LLOMe).
View Article and Find Full Text PDFJ Exp Bot
January 2025
Department of Botany and Plant Sciences, University of California, Riverside, CA 92521, USA.
SUPPRESSOR OF MAX2 1 (SMAX1) and SMAX1-LIKE (SMXL) proteins comprise a family of plant growth regulators that includes downstream targets of the karrikin (KAR)/KAI2 ligand (KL) and strigolactone (SL) signaling pathways. Following the perception of KAR/KL or SL signals by α/β hydrolases, some types of SMXL proteins are polyubiquitinated by an E3 ubiquitin ligase complex containing the F-box protein MORE AXILLARY GROWTH2 (MAX2)/DWARF3 (D3), and proteolyzed. Because SMXL proteins interact with TOPLESS (TPL) and TPL-related (TPR) transcriptional corepressors, SMXL degradation initiates changes in gene expression.
View Article and Find Full Text PDFCyclin F, a non-canonical member of the cyclin protein family, plays a critical role in regulating the precise transitions of cell-cycle events. Unlike canonical cyclins, which bind and activate cyclin-dependent kinases (CDKs), Cyclin F functions as a substrate receptor protein within the Skp1-Cullin-F box (SCF) E3 ubiquitin ligase complex, enabling the ubiquitylation of target proteins. The structural features that distinguish Cyclin F as a ligase adaptor and the mechanisms underlying its selective substrate recruitment over Cyclin A, which functions in complex with CDK2 at a similar time in the cell cycle, remain largely unexplored.
View Article and Find Full Text PDFInt J Mol Sci
January 2025
College of Grassland Science and Technology, Sichuan Agricultural University, Chengdu 611130, China.
As a crucial post-translational modification (PTM), protein ubiquitination mediates the breakdown of particular proteins, which plays a pivotal role in a large number of biological processes including plant growth, development, and stress response. The ubiquitin-proteasome system (UPS) consists of ubiquitin (Ub), ubiquitinase, deubiquitinating enzyme (DUB), and 26S proteasome mediates more than 80% of protein degradation for protein turnover in plants. For the ubiquitinases, including ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzyme (E2), and ubiquitin ligase (E3), the FBK (F-box Kelch repeat protein) is an essential component of multi-subunit E3 ligase SCF (Skp1-Cullin 1-F-box) involved in the specific recognition of target proteins in the UPS.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
January 2025
Beijing Key Laboratory of Growth and Developmental Regulation for Protected Vegetable Crops, College of Horticulture, China Agricultural University, Beijing 100193, China.
Light serves as an energy source for cell division and expansion during fruit development. Cell expansion significantly influences fruit size and is closely linked to endoreduplication, a unique cell cycle variation characterized by DNA replication without cytokinesis. Paradoxically, under conditions of ample photosynthates, light signaling suppresses cell expansion.
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