{"title":"Regulation of glycolysis and cancer cell proliferation by PKM2 citrullination.","authors":"Sébastien Coassolo, Irwin Davidson","doi":"10.1080/23723556.2021.1927446","DOIUrl":"https://doi.org/10.1080/23723556.2021.1927446","url":null,"abstract":"<p><p>Conversion of peptidyl-arginine to peptidyl citrulline, known as citrullination, is a post-translational protein modification catalyzed by the PADI (Protein Arginine Deiminase) family of enzymes. PADI1 and PADI3 catalyze citrullination of arginine 106 in the glycolytic enzyme pyruvate kinase M2 modulating its allosteric regulation, glycolysis and cancer cell proliferation.</p>","PeriodicalId":37292,"journal":{"name":"Molecular and Cellular Oncology","volume":"8 4","pages":"1927446"},"PeriodicalIF":2.1,"publicationDate":"2021-06-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/23723556.2021.1927446","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39492054","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The concerted action of oncogenic driver mutations directs global translation in intestinal epithelial cells.","authors":"Wouter Smit, Jarom Heijmans","doi":"10.1080/23723556.2021.1879614","DOIUrl":"https://doi.org/10.1080/23723556.2021.1879614","url":null,"abstract":"<p><p>Oncogenic transformation of colorectal cancer cells is driven by a set of mutations that cause aberrant signaling of growth factor-receptor pathways. Using organoids, we demonstrate that the most frequent driver mutations in <i>APC, KRAS, SMAD4</i>, and <i>TP53</i> are enhancers of the global mRNA translational capacity, which is linked to intestinal cell growth in an mTOR-dependent manner.</p>","PeriodicalId":37292,"journal":{"name":"Molecular and Cellular Oncology","volume":"8 4","pages":"1879614"},"PeriodicalIF":2.1,"publicationDate":"2021-05-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/23723556.2021.1879614","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39492050","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Yes, MAM!","authors":"Robert E Means, Samuel G Katz","doi":"10.1080/23723556.2021.1919473","DOIUrl":"https://doi.org/10.1080/23723556.2021.1919473","url":null,"abstract":"<p><p>Regulation of cell life and death by members of the BCL-2 family of proteins occurs at the mitochondria. Large portions of the mitochondria's outer membrane are found in tight approximation with the endoplasmic reticulum (ER), known as mitochondria-associated membranes (MAMs) or mitochondria-ER contact sites (MERCs). We recently reported that BOK is present within MAMs where it regulates Ca<sup>2+</sup> transfer from the ER to the mitochondria, appropriate MAM components and MERC structure, and apoptosis.</p>","PeriodicalId":37292,"journal":{"name":"Molecular and Cellular Oncology","volume":"8 4","pages":"1919473"},"PeriodicalIF":2.1,"publicationDate":"2021-05-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/23723556.2021.1919473","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39492052","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Regulation of nuclear mTORC1.","authors":"Xin Zhou, Yanghao Zhong, Jin Zhang","doi":"10.1080/23723556.2021.1896348","DOIUrl":"https://doi.org/10.1080/23723556.2021.1896348","url":null,"abstract":"<p><p>mTORC1 integrates diverse upstream signals to control cell growth and metabolism. We previously showed that mTORC1 activity is spatially compartmentalized to ensure its signaling specificity. In a recently published study, we demonstrated the existence of mTORC1 activity in the nucleus and identified a unique mode of its regulation in the nuclear compartment.</p>","PeriodicalId":37292,"journal":{"name":"Molecular and Cellular Oncology","volume":"8 3","pages":"1896348"},"PeriodicalIF":2.1,"publicationDate":"2021-05-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/23723556.2021.1896348","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39010559","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Regulation of autophagy by VPS34 branched ubiquitination controls proteostasis and liver metabolism.","authors":"Yu-Hsuan Chen, Ruey-Hwa Chen","doi":"10.1080/23723556.2021.1915076","DOIUrl":"https://doi.org/10.1080/23723556.2021.1915076","url":null,"abstract":"<p><p>Ubiquitin-proteasome system and autophagy are the two major recycling processes. Our recent work uncovers a K29/K48 branched ubiquitination on the phosphatidylinositol 3-kinase catalytic subunit type 3 (PI3KC3, best known as VPS34). This ubiquitination is positively or negatively regulated under pathophysiological conditions to influence on autophagy, proteostasis and lipid homeostasis.</p>","PeriodicalId":37292,"journal":{"name":"Molecular and Cellular Oncology","volume":"8 3","pages":"1915076"},"PeriodicalIF":2.1,"publicationDate":"2021-05-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/23723556.2021.1915076","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39012049","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"<i>FOXA1</i> mutations influence the therapeutic response of breast cancer by altering chromatin state.","authors":"Amaia Arruabarrena-Aristorena, Eneda Toska","doi":"10.1080/23723556.2021.1891831","DOIUrl":"https://doi.org/10.1080/23723556.2021.1891831","url":null,"abstract":"ABSTRACT Forkhead box protein A1 (FOXA1) is a pioneer transcription factor that contributes to chromatin opening to allow binding of estrogen receptor (ER) in ER+ breast cancer. Mutations in FOXA1 are recurrent in breast cancer but the functional consequences of these mutations remain unknown. We identified that FOXA1 mutations are associated with worse outcomes to endocrine therapy by inducing alternative chromatin profiles and gene activity in breast cancer.","PeriodicalId":37292,"journal":{"name":"Molecular and Cellular Oncology","volume":"8 3","pages":"1891831"},"PeriodicalIF":2.1,"publicationDate":"2021-05-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/23723556.2021.1891831","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39010557","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The importance of transmembrane domain interactions in the viral control of apoptosis.","authors":"Gerard Duart, Ismael Mingarro, Luis Martinez-Gil","doi":"10.1080/23723556.2021.1911290","DOIUrl":"https://doi.org/10.1080/23723556.2021.1911290","url":null,"abstract":"<p><p>Viral control of apoptosis occurs through the expression of viral encoded anti-apoptotic B-cell lymphoma 2 (BCL2) analogs. These proteins are thought to restrain apoptosis by interacting with cellular BCL2 family members. We identified that protein-protein interactions between cellular and viral BCL2 transmembrane domains are crucial for the viral protein's function.</p>","PeriodicalId":37292,"journal":{"name":"Molecular and Cellular Oncology","volume":"8 3","pages":"1911290"},"PeriodicalIF":2.1,"publicationDate":"2021-05-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/23723556.2021.1911290","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39012046","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Zmat3 splices together p53-dependent tumor suppression.","authors":"Kathryn T Bieging-Rolett, Laura D Attardi","doi":"10.1080/23723556.2021.1898523","DOIUrl":"https://doi.org/10.1080/23723556.2021.1898523","url":null,"abstract":"<p><p>The tumor protein p53 (TP53, best known as p53) transcription factor is a critical tumor suppressor, but those p53-inducible genes most important for tumor suppression have remained unclear. Using unbiased RNA interference and CRISPR (Clustered Regularly Interspersed Palindromic Repeats)/Cas9 (CRISPR-associated protein 9) screens, genetically engineered mouse models, human cancer genome analysis, and integrative eCLIP-sequencing and RNA-sequencing analyses, we reveal a new branch of p53-mediated tumor suppression involving the RNA splicing regulator Zinc finger Matrin-type 3, Zmat3.</p>","PeriodicalId":37292,"journal":{"name":"Molecular and Cellular Oncology","volume":"8 3","pages":"1898523"},"PeriodicalIF":2.1,"publicationDate":"2021-04-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/23723556.2021.1898523","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39010561","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"A mTORC1-mediated cyst(e)ine sensing mechanism governing GPX4 synthesis and ferroptosis.","authors":"Yuelong Yan, Guang Lei, Boyi Gan","doi":"10.1080/23723556.2021.1919006","DOIUrl":"https://doi.org/10.1080/23723556.2021.1919006","url":null,"abstract":"<p><p>Ferroptosis is a cell death mechanism triggered by lipid peroxidation. Our recent study linked cyst(e)ine availability with glutathione peroxidase 4 (GPX4) protein synthesis and ferroptosis mitigation via a Rag-mechanistic target of rapamycin complex 1 (mTORC1) axis, and proposed that co-targeting mTORC1 and ferroptosis is a promising strategy for cancer therapy.</p>","PeriodicalId":37292,"journal":{"name":"Molecular and Cellular Oncology","volume":"8 3","pages":"1919006"},"PeriodicalIF":2.1,"publicationDate":"2021-04-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/23723556.2021.1919006","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39012050","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"HDAC2 links ubiquitination to tumor suppression in synovial sarcoma.","authors":"Christina Cooley, Le Su","doi":"10.1080/23723556.2021.1914291","DOIUrl":"https://doi.org/10.1080/23723556.2021.1914291","url":null,"abstract":"<p><p>The function of histone deacetylase 2 (HDAC2) in transcriptional regulation and its role in oncogenesis have been well established. Here we discuss a transcription-independent HDAC2 pathway controlling cancer-related protein stability via the mouse double minute 2 homolog (MDM2) ubiquitin ligase. In synovial sarcoma, HDAC2 inactivation demonstrates significant therapeutic effect by degradation of the SS18-SSX driver oncoprotein.</p>","PeriodicalId":37292,"journal":{"name":"Molecular and Cellular Oncology","volume":"8 3","pages":"1914291"},"PeriodicalIF":2.1,"publicationDate":"2021-04-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/23723556.2021.1914291","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39012047","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}