{"title":"The lipid phosphatase INPP4B controls pancreatic cancer cell migration and invasion by regulating fibronectin exocytosis.","authors":"Golam T Saffi,Nicholas Kleine,Leonardo Salmena","doi":"10.1016/j.jbc.2025.110716","DOIUrl":"https://doi.org/10.1016/j.jbc.2025.110716","url":null,"abstract":"Increased expression of Inositol Polyphosphate 4-Phosphatase, Type II (INPP4B) correlates with aggressive phenotypes in pancreatic ductal adenocarcinoma (PDAC). Although prior studies have linked INPP4B to lysosome positioning, exocytosis, and enhanced cell migration and invasion in PDAC, the specific mechanisms underlying these processes remain unclear. In this study, we demonstrate that INPP4B promotes fibronectin 1 (FN1) secretion via TRPML1-dependent lysosomal exocytosis. Additionally, we show that INPP4B-mediated regulation of F-actin formation, focal adhesion kinase (FAK) activation, and increased cell migration and invasion depend on FN1 exocytosis. These findings underscore the INPP4B-TRPML1-FN1 axis as a critical contributor to PDAC aggressiveness and identify it as a promising candidate for the development of new therapeutic strategies.","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"56 1","pages":"110716"},"PeriodicalIF":4.8,"publicationDate":"2025-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145078279","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The Complex Network of p300/CBP Regulation: Interactions, Post-Translational Modifications, and Therapeutic Implications.","authors":"Ebru Yazıcı,Justyna McIntyre","doi":"10.1016/j.jbc.2025.110715","DOIUrl":"https://doi.org/10.1016/j.jbc.2025.110715","url":null,"abstract":"Two closely related acetyltransferases, p300 and its paralogue CBP, are important regulators of gene expression and protein modulators in higher eukaryotes, influencing a wide array of cellular processes, including cell division, growth, DNA replication and repair, and apoptosis. The broad cellular impact is underscored by p300/CBP's capacity to interact with hundreds of proteins through various domains and the capability to acetylate numerous substrates and ubiquitinate selected targets. This intricate network of interactions and modifications, highlights the essential role of p300/CBP in orchestrating cellular responses to pathological and physiological stimuli, thereby necessitating precise regulatory mechanisms to maintain their activity and substrate specificity. The regulation of p300/CBP is primarily governed by protein interactions and post-translational modifications, including acetylation and ubiquitination, with autoregulation serving as a vital component in sustaining their enzymatic functions. The significance of tightly controlled p300/CBP activity is further emphasized by its association with various diseases, including Rubinstein-Taybi syndrome, Menke-Hennekam syndrome, and numerous cancers. Furthermore, the potential of p300/CBP as a therapeutic target has sparked interest in developing specific inhibitors. This review aims to elucidate the complex regulatory mechanisms of p300/CBP, focusing on post-translational modifications, intermolecular interactions, and their implications in disease. A comprehensive understanding of the molecular foundations of p300/CBP regulation is essential for unraveling their roles in cellular processes and advancing targeted therapeutic strategies.","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"66 1","pages":"110715"},"PeriodicalIF":4.8,"publicationDate":"2025-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145078282","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Alexander V Peskin, Flavia C Meotti, Nicholas J Magon, Luiz F de Souza, Armindo Salvador, Christine C Winterbourn
{"title":"Correction: Mechanism of glutathionylation of the active site thiols of peroxiredoxin 2.","authors":"Alexander V Peskin, Flavia C Meotti, Nicholas J Magon, Luiz F de Souza, Armindo Salvador, Christine C Winterbourn","doi":"10.1016/j.jbc.2025.110628","DOIUrl":"https://doi.org/10.1016/j.jbc.2025.110628","url":null,"abstract":"","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"301 10","pages":"110628"},"PeriodicalIF":4.0,"publicationDate":"2025-09-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145069508","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Sivaprakasam Balasubramanian, Ling Zhu, Richard L Eckert
{"title":"Correction: Apigenin inhibition of involucrin gene expression is associated with a specific reduction in phosphorylation of protein kinase Cδ tyr<sup>311</sup>.","authors":"Sivaprakasam Balasubramanian, Ling Zhu, Richard L Eckert","doi":"10.1016/j.jbc.2025.110624","DOIUrl":"https://doi.org/10.1016/j.jbc.2025.110624","url":null,"abstract":"","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"301 10","pages":"110624"},"PeriodicalIF":4.0,"publicationDate":"2025-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145064698","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Kamalika Saha, Gautam Adhikary, Santosh R Kanade, Ellen A Rorke, Richard L Eckert
{"title":"Withdrawal: p38δ regulates p53 to control p21<sup>Cip1</sup> expression in human epidermal keratinocytes.","authors":"Kamalika Saha, Gautam Adhikary, Santosh R Kanade, Ellen A Rorke, Richard L Eckert","doi":"10.1016/j.jbc.2025.110621","DOIUrl":"10.1016/j.jbc.2025.110621","url":null,"abstract":"","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"301 10","pages":"110621"},"PeriodicalIF":4.0,"publicationDate":"2025-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145064742","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Correction: Protein arginine methyltransferase 5 (PRMT5) signaling suppresses protein kinase Cδ- and p38δ-dependent signaling and keratinocyte differentiation.","authors":"Santosh R Kanade, Richard L Eckert","doi":"10.1016/j.jbc.2025.110626","DOIUrl":"https://doi.org/10.1016/j.jbc.2025.110626","url":null,"abstract":"","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"301 10","pages":"110626"},"PeriodicalIF":4.0,"publicationDate":"2025-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145064744","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Correction: Curcumin suppresses AP1 transcription factor-dependent differentiation and activates apoptosis in human epidermal keratinocytes.","authors":"Sivaprakasam Balasubramanian, Richard L Eckert","doi":"10.1016/j.jbc.2025.110625","DOIUrl":"https://doi.org/10.1016/j.jbc.2025.110625","url":null,"abstract":"","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"301 10","pages":"110625"},"PeriodicalIF":4.0,"publicationDate":"2025-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145064722","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Withdrawal: A regulatory role for p38δ MAPK in keratinocyte differentiation: Evidence for p38δ-ERK1/2 complex formation.","authors":"Tatiana Efimova,Ann-Marie Broome,Richard L Eckert","doi":"10.1016/j.jbc.2025.110619","DOIUrl":"https://doi.org/10.1016/j.jbc.2025.110619","url":null,"abstract":"","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"36 1","pages":"110619"},"PeriodicalIF":4.8,"publicationDate":"2025-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145058927","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Withdrawal: Methylosome protein 50 and PKCδ/p38δ protein signaling control keratinocyte proliferation via opposing effects on p21<sup>Cip1</sup> gene expression.","authors":"Kamalika Saha, Richard L Eckert","doi":"10.1016/j.jbc.2025.110622","DOIUrl":"10.1016/j.jbc.2025.110622","url":null,"abstract":"","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"301 10","pages":"110622"},"PeriodicalIF":4.0,"publicationDate":"2025-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145064732","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Yap Ching Chew, Gautam Adhikary, Gerald M Wilson, E Albert Reece, Richard L Eckert
{"title":"Withdrawal: Protein Kinase C (PKC) δ suppresses keratinocyte proliferation by increasing p21Cip1 level by a KLF4 transcription factor-dependent mechanism.","authors":"Yap Ching Chew, Gautam Adhikary, Gerald M Wilson, E Albert Reece, Richard L Eckert","doi":"10.1016/j.jbc.2025.110620","DOIUrl":"10.1016/j.jbc.2025.110620","url":null,"abstract":"","PeriodicalId":15140,"journal":{"name":"Journal of Biological Chemistry","volume":"301 10","pages":"110620"},"PeriodicalIF":4.0,"publicationDate":"2025-09-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145064769","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}