AI Article Synopsis
- 14-3-3 proteins are essential cellular proteins that help regulate important physiological processes, including cell growth, survival, and the cell cycle.
- Over 200 target proteins of 14-3-3 have been identified, many of which are linked to cancer development through their regulation of oncogenes and tumor suppressor genes.
- The review discusses recent research on the role of 14-3-3 proteins in cancer, exploring how they contribute to tumor development and progression.
Article Abstract
14-3-3 proteins are a family of highly conserved cellular proteins that play key roles in the regulation of central physiological pathways. More than 200 14-3-3 target proteins have been identified, including proteins involved in mitogenic and cell survival signaling, cell cycle control and apoptotic cell death. Importantly, the involvement of 14-3-3 proteins in the regulation of various oncogenes and tumor suppressor genes points to a potential role in human cancer. The present review summarizes current findings implicating a 14-3-3 role in cancer while discussing potential mechanisms and points of action of 14-3-3 during cancer development and progression.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.semcancer.2006.03.004 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Background: Nearly all people with Down Syndrome (DS) develop Alzheimer's dementia (AD) by the 7 decade of life. However, whether the alterations in fluid biomarker levels associated with DS follow the same pattern to those observed in other forms of AD is not well understood.
Method: We used mass spectrometry-based proteomics to measure 1116 proteins in cerebrospinal fluid (CSF) across euploid controls (n=130), sporadic late-onset AD (LOAD, n=89), asymptomatic DS (n=117), prodromal DS (n=57), and dementia DS (n=80) cases, and compared the protein changes observed in DS to those in LOAD and to those recently described in autosomal dominant AD (ADAD).
as an oral bacteria promotes the carcinogenesis of laryngeal cancer via upregulating YWHAZ.
J Oral Microbiol
December 2024
School of Medicine, Zhejiang University, Hangzhou, Zhejiang, China.
Background And Purpose: F. nucleatum, a gram-negative oral bacteria, is abundant in laryngeal cancer (LC). While specific 14-3-3 proteins act as LC oncogenes, the link between F.
View Article and Find Full Text PDFLigand recognition by 14-3-3 proteins requires negative charges but not necessarily phosphorylation.
FEBS Lett
January 2025
Department of Biomedical Sciences, Creighton University, Omaha, NE, USA.
Protein-protein interactions involving 14-3-3 proteins regulate various cellular activities in normal and pathological conditions. These interactions have mostly been reported to be phosphorylation-dependent, but the 14-3-3 proteins also interact with unphosphorylated proteins. In this work, we investigated whether phosphorylation is required, or, alternatively, whether negative charges are sufficient for 14-3-3ε binding.
View Article and Find Full Text PDFNHSL3 controls single and collective cell migration through two distinct mechanisms.
Nat Commun
January 2025
Laboratory of Structural Biology of the Cell (BIOC), CNRS UMR7654, École Polytechnique, Institut Polytechnique de Paris, Palaiseau, France.
The molecular mechanisms underlying cell migration remain incompletely understood. Here, we show that knock-out cells for NHSL3, the most recently identified member of the Nance-Horan Syndrome family, are more persistent than parental cells in single cell migration, but that, in wound healing, follower cells are impaired in their ability to follow leader cells. The NHSL3 locus encodes several isoforms.
View Article and Find Full Text PDFYAP K236 acetylation facilitates its nucleic export and deprived the protection against cardiac hypertrophy in mice.
Pharmacol Res
December 2024
Guangzhou Municipal and Guangdong Provincial Key Laboratory of Molecular Target & Clinical Pharmacology, the NMPA and State Key Laboratory of Respiratory Disease, School of Pharmaceutical Sciences, Guangzhou Medical University, Guangzhou 511436, PR China. Electronic address:
The subcellular localization of Yes-associated protein (YAP) is dynamically regulated by post-transcriptional modifications, critically influencing cardiac function. Despite its significance, the precise mechanism controlling YAP nuclear sequestration and its role in cardiac hypertrophy remain poorly defined. In this study, utilizing immunoprecipitation-mass spectrometry, we identified potential acetylation sites and interacting proteins of YAP.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!