{"title":"TRIM44 as a Multifunctional Regulator in Cancer and Non-Cancer Diseases: From Oncogenic Driver to Immune and Stress Response Modulator.","authors":"Guive Sharifi, Tohid Emami Meybodi, Fatemeh Jayervand, Mahmood Emami Meybodi, Khatere Mokhtari, Parnaz Mohseni, Hanie Mahaki, Hamidreza Hasanzadeh, Elham Bateni, Yaser Sharafi, Farzan Fahim, Ahmad Hemmatyar, Esmaeil Mohammadi, Maryam Ahmadi, Majid Jahanshahi, Hamid Tanzadehpanah","doi":"10.2174/0109298665428424251216064630","DOIUrl":null,"url":null,"abstract":"<p><p>Tripartite motif-containing protein 44 (TRIM44), a unique member of the TRIM family that lacks the canonical RING domain, has recently attracted significant attention for its broad oncogenic potential across diverse malignancies. Accumulating evidence indicates that TRIM44 is markedly overexpressed in cancers, including colorectal, gastric, lung, breast, ovarian, and prostate carcinomas, as well as glioblastoma, multiple myeloma, and hepatocellular carcinoma. Mechanistically, TRIM44 drives tumor progression by modulating critical signaling pathways, including PI3K/AKT/mTOR, NF-κB, Wnt/β-catenin, and epithelial-mesenchymal transition (EMT), primarily through stabilizing regulatory proteins or participating in non-coding RNA- mediated networks. In addition to its role in cancer, TRIM44 has been implicated in cardiovascular dysfunction, ischemia-reperfusion injury, diabetic complications, and neuroinflammation, underscoring its biological versatility. This review provides an overview of current evidence regarding the multifaceted roles of TRIM44 in both oncogenic and non-oncogenic diseases. By integrating insights from oncology, cardiology, neurology, and metabolic research, this review offers a unified perspective on TRIM44 as a pivotal molecular hub and an emerging diagnostic and therapeutic target.</p>","PeriodicalId":20736,"journal":{"name":"Protein and Peptide Letters","volume":" ","pages":"79-97"},"PeriodicalIF":2.5000,"publicationDate":"2026-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Protein and Peptide Letters","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.2174/0109298665428424251216064630","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Tripartite motif-containing protein 44 (TRIM44), a unique member of the TRIM family that lacks the canonical RING domain, has recently attracted significant attention for its broad oncogenic potential across diverse malignancies. Accumulating evidence indicates that TRIM44 is markedly overexpressed in cancers, including colorectal, gastric, lung, breast, ovarian, and prostate carcinomas, as well as glioblastoma, multiple myeloma, and hepatocellular carcinoma. Mechanistically, TRIM44 drives tumor progression by modulating critical signaling pathways, including PI3K/AKT/mTOR, NF-κB, Wnt/β-catenin, and epithelial-mesenchymal transition (EMT), primarily through stabilizing regulatory proteins or participating in non-coding RNA- mediated networks. In addition to its role in cancer, TRIM44 has been implicated in cardiovascular dysfunction, ischemia-reperfusion injury, diabetic complications, and neuroinflammation, underscoring its biological versatility. This review provides an overview of current evidence regarding the multifaceted roles of TRIM44 in both oncogenic and non-oncogenic diseases. By integrating insights from oncology, cardiology, neurology, and metabolic research, this review offers a unified perspective on TRIM44 as a pivotal molecular hub and an emerging diagnostic and therapeutic target.
期刊介绍:
Protein & Peptide Letters publishes letters, original research papers, mini-reviews and guest edited issues in all important aspects of protein and peptide research, including structural studies, advances in recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, and drug design. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallization and preliminary structure determination of biologically important proteins are considered only if they include significant new approaches or deal with proteins of immediate importance, and preliminary structure determinations of biologically important proteins. Purely theoretical/review papers should provide new insight into the principles of protein/peptide structure and function. Manuscripts describing computational work should include some experimental data to provide confirmation of the results of calculations.
Protein & Peptide Letters focuses on:
Structure Studies
Advances in Recombinant Expression
Drug Design
Chemical Synthesis
Function
Pharmacology
Enzymology
Conformational Analysis
Immunology
Biotechnology
Protein Engineering
Protein Folding
Sequencing
Molecular Recognition
Purification and Analysis