{"title":"EXPRESSION OF CONCERN: Nrf2 Dependent Antiaging Effect of Milk-Derived Bioactive Peptide in Old Fibroblasts.","authors":"","doi":"10.1002/jcb.30666","DOIUrl":"10.1002/jcb.30666","url":null,"abstract":"","PeriodicalId":15219,"journal":{"name":"Journal of cellular biochemistry","volume":" ","pages":"e30666"},"PeriodicalIF":3.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142380938","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Natalia M Galigniana, Marina C Ruiz, Graciela Piwien-Pilipuk
{"title":"FK506 binding protein 51: Its role in the adipose organ and beyond.","authors":"Natalia M Galigniana, Marina C Ruiz, Graciela Piwien-Pilipuk","doi":"10.1002/jcb.30351","DOIUrl":"10.1002/jcb.30351","url":null,"abstract":"<p><p>There is a great body of evidence that the adipose organ plays a central role in the control not only of energy balance, but importantly, in the maintenance of metabolic homeostasis. Interest in the study of different aspects of its physiology grew in the last decades due to the pandemic of obesity and the consequences of metabolic syndrome. It was not until recently that the first evidence for the role of the high molecular weight immunophilin FK506 binding protein (FKBP) 51 in the process of adipocyte differentiation have been described. Since then, many new facets have been discovered of this stress-responsive FKBP51 as a central node for precise coordination of many cell functions, as shown for nuclear steroid receptors, autophagy, signaling pathways as Akt, p38 MAPK, and GSK3, as well as for insulin signaling and the control of glucose homeostasis. Thus, the aim of this review is to integrate and discuss the recent advances in the understanding of the many roles of FKBP51 in the adipose organ.</p>","PeriodicalId":15219,"journal":{"name":"Journal of cellular biochemistry","volume":" ","pages":"e30351"},"PeriodicalIF":3.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10435531","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Asat Baischew, Sarah Engel, Thomas M Geiger, Martha C Taubert, Felix Hausch
{"title":"Structural and biochemical insights into FKBP51 as a Hsp90 co-chaperone.","authors":"Asat Baischew, Sarah Engel, Thomas M Geiger, Martha C Taubert, Felix Hausch","doi":"10.1002/jcb.30384","DOIUrl":"10.1002/jcb.30384","url":null,"abstract":"<p><p>The FK506-binding protein 51 (FKBP51) is a high-molecular-weight immunophilin that emerged as an important drug target for stress-related disorders, chronic pain, and obesity. It has been implicated in a plethora of molecular pathways but remains best characterized as a co-chaperone of Hsp90 in the steroid hormone receptor (SHR) maturation cycle. However, the mechanistic and structural basis for the regulation of SHRs by FKBP51 and the usually antagonistic function compared with its closest homolog FKBP52 remains enigmatic. Here we review recent structural and biochemical studies of FKBPs as regulators in the Hsp90 machinery. These advances provide important insights into the roles of FKBP51 and FKBP52 in SHR regulation.</p>","PeriodicalId":15219,"journal":{"name":"Journal of cellular biochemistry","volume":" ","pages":"e30384"},"PeriodicalIF":3.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10787794","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"RETRACTION: Downregulation of Fibroblast Growth Factor 5 Inhibits Cell Growth and Invasion of Human Nonsmall-Cell Lung Cancer Cells.","authors":"","doi":"10.1002/jcb.30673","DOIUrl":"10.1002/jcb.30673","url":null,"abstract":"","PeriodicalId":15219,"journal":{"name":"Journal of cellular biochemistry","volume":" ","pages":"e30673"},"PeriodicalIF":3.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142603299","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Olga B Soto, Christian S Ramirez, Rina Koyani, Isela A Rodriguez-Palomares, Jessica R Dirmeyer, Brian Grajeda, Sourav Roy, Marc B Cox
{"title":"Structure and function of the TPR-domain immunophilins FKBP51 and FKBP52 in normal physiology and disease.","authors":"Olga B Soto, Christian S Ramirez, Rina Koyani, Isela A Rodriguez-Palomares, Jessica R Dirmeyer, Brian Grajeda, Sourav Roy, Marc B Cox","doi":"10.1002/jcb.30406","DOIUrl":"10.1002/jcb.30406","url":null,"abstract":"<p><p>Coordinated cochaperone interactions with Hsp90 and associated client proteins are crucial for a multitude of signaling pathways in normal physiology, as well as in disease settings. Research on the molecular mechanisms regulated by the Hsp90 multiprotein complexes has demonstrated increasingly diverse roles for cochaperones throughout Hsp90-regulated signaling pathways. Thus, the Hsp90-associated cochaperones have emerged as attractive therapeutic targets in a wide variety of disease settings. The tetratricopeptide repeat (TPR)-domain immunophilins FKBP51 and FKBP52 are of special interest among the Hsp90-associated cochaperones given their Hsp90 client protein specificity, ubiquitous expression across tissues, and their increasingly important roles in neuronal signaling, intracellular calcium release, peptide bond isomerization, viral replication, steroid hormone receptor function, and cell proliferation to name a few. This review summarizes the current knowledge of the structure and molecular functions of TPR-domain immunophilins FKBP51 and FKBP52, recent findings implicating these immunophilins in disease, and the therapeutic potential of targeting FKBP51 and FKBP52 for the treatment of disease.</p>","PeriodicalId":15219,"journal":{"name":"Journal of cellular biochemistry","volume":" ","pages":"e30406"},"PeriodicalIF":3.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10903107/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9755081","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The animal and cell models that uncovered FKBP51 as a regulator of glucocorticoid receptor function.","authors":"Jonathan G Scammell","doi":"10.1002/jcb.30375","DOIUrl":"10.1002/jcb.30375","url":null,"abstract":"<p><p>Many New World primates are glucocorticoid-resistant secondary to expression of low affinity glucocorticoid receptors. We identified the role of FKBP51 in hormone responsiveness by showing that multiple cell lines derived from New World primates share the same activities: (1) soluble cell extracts conferred low binding affinity to high affinity glucocorticoid receptors; (2) FK506 increased receptor binding in soluble cell extracts; and (3) cellular FKBP51 was elevated and FKBP52 was lower. Details of these cell lines and their availability are described. Subsequently, we showed that New World primate and human FKBP51 decreased glucocorticoid activity in heterologous COS-7 cell cultures. Future studies using the FKBP51 antagonist SAFit2 in New World primates are proposed.</p>","PeriodicalId":15219,"journal":{"name":"Journal of cellular biochemistry","volume":" ","pages":"e30375"},"PeriodicalIF":3.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9188827","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"RETRACTION: Trans-Cleaving Hammerhead Ribozyme in Specific Regions Can Improve Knockdown Efficiency In Vivo.","authors":"","doi":"10.1002/jcb.30677","DOIUrl":"10.1002/jcb.30677","url":null,"abstract":"<p><strong>Retraction: </strong>Y. Peng, X. Ai, and B. Peng, \"Trans-cleaving Hammerhead Ribozyme in Specific Regions Can Improve Knockdown Efficiency In Vivo,\" Journal of Cellular Biochemistry (Early View): https://doi.org/10.1002/jcb.30249. The above article, published online on 11 April 2022 in Wiley Online Library (wileyonlinelibrary.com), has been retracted by agreement between the authors; the journal Editor-in-Chief, Christian Behl; and Wiley Periodicals LLC. The retraction has been agreed upon the authors' request due to concerns related to the data presented in the article. The authors admitted significant errors in the evaluation of the fluorescence intensity, resulting in inaccurate data on the trans-cleaving efficiency of the presented system. They also informed the journal of errors in the results of the immunoblot assays. As the identified errors affect the overall conclusions of the study, the article is retracted.</p>","PeriodicalId":15219,"journal":{"name":"Journal of cellular biochemistry","volume":" ","pages":"e30677"},"PeriodicalIF":3.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142620374","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Genetically engineered mouse models of FK506-binding protein 5.","authors":"Niat T Gebru, Shannon E Hill, Laura J Blair","doi":"10.1002/jcb.30374","DOIUrl":"10.1002/jcb.30374","url":null,"abstract":"<p><p>FK506 binding protein 51 (FKBP51) is a molecular chaperone that influences stress response. In addition to having an integral role in the regulation of steroid hormone receptors, including glucocorticoid receptor, FKBP51 has been linked with several biological processes including metabolism and neuronal health. Genetic and epigenetic alterations in the gene that encodes FKBP51, FKBP5, are associated with increased susceptibility to multiple neuropsychiatric disorders, which has fueled much of the research on this protein. Because of the complexity of these processes, animal models have been important in understanding the role of FKBP51. This review examines each of the current mouse models of FKBP5, which include whole animal knockout, conditional knockout, overexpression, and humanized mouse models. The generation of each model and observational details are discussed, including behavioral phenotypes, molecular changes, and electrophysiological alterations basally and following various challenges. While much has been learned through these models, there are still many aspects of FKBP51 biology that remain opaque and future studies are needed to help illuminate these current gaps in knowledge. Overall, FKBP5 continues to be an exciting potential target for stress-related disorders.</p>","PeriodicalId":15219,"journal":{"name":"Journal of cellular biochemistry","volume":" ","pages":"e30374"},"PeriodicalIF":3.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10423308/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10346775","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Lazar M Vasović, Gordana M Pavlović-Lažetić, Jovana J Kovačević, Miloš V Beljanski, Vladimir N Uversky
{"title":"Intrinsically disordered proteins and liquid-liquid phase separation in SARS-CoV-2 interactomes.","authors":"Lazar M Vasović, Gordana M Pavlović-Lažetić, Jovana J Kovačević, Miloš V Beljanski, Vladimir N Uversky","doi":"10.1002/jcb.30502","DOIUrl":"10.1002/jcb.30502","url":null,"abstract":"<p><p>This paper discusses the properties of proteins and their relations in the interactomes of the selected subsets of SARS-CoV-2 proteome-the membrane protein, nonstructural proteins, and, finally, full proteome. Protein disorder according to several measures, liquid-liquid phase separation probabilities, and protein node degrees in the interaction networks were singled out as the features of interest. Additionally, viral interactomes were combined with the interactome of human lung tissue so as to examine if the new connections in the resulting viral-host interactome are linked to protein disorder. Correlation analysis shows that there is no clear relationship between raw features of interest, whereas there is a positive correlation between the protein disorder and its neighborhood mean disorder. There are also indications that highly connected viral hubs tend to be on average more ordered than proteins with a small number of connections. This is in contrast to previous similar studies conducted on eukaryotic interactomes and possibly raises new questions in research on viral interactomes.</p>","PeriodicalId":15219,"journal":{"name":"Journal of cellular biochemistry","volume":" ","pages":"e30502"},"PeriodicalIF":3.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138295238","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Heterogeneous nuclear ribonucleoprotein A3 binds to the internal ribosomal entry site of enterovirus A71 and affects virus replication in neural cells.","authors":"Jhao-Yin Lin, Jing-Yi Lin, Rei-Lin Kuo, Hsing-I Huang","doi":"10.1002/jcb.30575","DOIUrl":"10.1002/jcb.30575","url":null,"abstract":"<p><p>Enterovirus A71 (EV-A71) belongs to the genus Enterovirus of the Picornaviridae family and often causes outbreaks in Asia. EV-A71 infection usually causes hand, foot, and mouth disease and can even affect the central nervous system, causing neurological complications or death. The 5'-untranslated region (5'-UTR) of EV-A71 contains an internal ribosome entry site (IRES) that is responsible for the translation of viral proteins. IRES-transacting factors can interact with the EV-A71 5'-UTR to regulate IRES activity. Heterogeneous nuclear ribonucleoprotein (hnRNP) A3 is a member of the hnRNP A/B protein family of RNA-binding proteins and is involved in RNA transport and modification. We found that hnRNP A3 knockdown promoted the replication of EV-A71 in neural calls. Conversely, increasing the expression of hnRNP A3 within cells inhibits the growth of EV-A71. HnRNP A3 can bind to the EV-A71 5'-UTR, and knockdown of hnRNP A3 enhances the luciferase activity of the EV-A71 5'-UTR IRES. The localization of hnRNP A3 shifts from the nucleus to the cytoplasm of infected cells during viral infection. Additionally, EV-A71 infection can increase the protein expression of hnRNP A3, and the protein level is correlated with efficient viral growth. Based on these findings, we concluded that hnRNP A3 plays a negative regulatory role in EV-A71 replication within neural cells.</p>","PeriodicalId":15219,"journal":{"name":"Journal of cellular biochemistry","volume":" ","pages":"e30575"},"PeriodicalIF":3.0,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140891653","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}