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Article ; Online: Subcellular Fractionation Suitable for Studies of RNA and Protein Trafficking.

Culjkovic-Kraljacic, Biljana / Borden, Katherine L B

Methods in molecular biology (Clifton, N.J.)

2022 Volume 2502, Page(s) 91–104

Abstract: The nuclear pore complex is the major conduit for trafficking between the nucleus and cytoplasm. Nuclear import and export of both proteins and RNAs represent important functional steps for many biological processes. One of the major means to study NPC ... ...

Abstract	The nuclear pore complex is the major conduit for trafficking between the nucleus and cytoplasm. Nuclear import and export of both proteins and RNAs represent important functional steps for many biological processes. One of the major means to study NPC activity and the nuclear and cytoplasmic distribution of proteins and RNAs is through biochemical fractionation. Here, we describe detailed methods to generate high quality nuclear and cytoplasmic fractions simultaneously capturing RNA and proteins which can be used subsequently for a wide array of biochemical characterizations including proteomics and next generation sequencings.
MeSH term(s)	Active Transport, Cell Nucleus ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; Nuclear Pore/metabolism ; Protein Transport ; RNA/metabolism
Chemical Substances	RNA (63231-63-0)
Language	English
Publishing date	2022-04-12
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-2337-4_6
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Article: The Cap-Binding Complex CBC and the Eukaryotic Translation Factor eIF4E: Co-Conspirators in Cap-Dependent RNA Maturation and Translation.

Mars, Jean-Clement / Ghram, Mehdi / Culjkovic-Kraljacic, Biljana / Borden, Katherine L B

Cancers

2021 Volume 13, Issue 24

Abstract: The translation of RNA into protein is a dynamic process which is heavily regulated during normal cell physiology and can be dysregulated in human malignancies. Its dysregulation can impact selected groups of RNAs, modifying protein levels independently ... ...

Abstract	The translation of RNA into protein is a dynamic process which is heavily regulated during normal cell physiology and can be dysregulated in human malignancies. Its dysregulation can impact selected groups of RNAs, modifying protein levels independently of transcription. Integral to their suitability for translation, RNAs undergo a series of maturation steps including the addition of the m
Language	English
Publishing date	2021-12-08
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2527080-1
ISSN	2072-6694
ISSN	2072-6694
DOI	10.3390/cancers13246185
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Article: The Impact of Post-transcriptional Control: Better Living Through RNA Regulons.

Culjkovic-Kraljacic, Biljana / Borden, Katherine L B

Frontiers in genetics

2018 Volume 9, Page(s) 512

Abstract: Traditionally, cancer is viewed as a disease driven by genetic mutations and/or epigenetic and transcriptional dysregulation. While these are undoubtedly important drivers, many recent studies highlight the disconnect between the proteome and the genome ... ...

Abstract	Traditionally, cancer is viewed as a disease driven by genetic mutations and/or epigenetic and transcriptional dysregulation. While these are undoubtedly important drivers, many recent studies highlight the disconnect between the proteome and the genome or transcriptome. At least in part, this disconnect arises as a result of dysregulated RNA metabolism which underpins the altered proteomic landscape observed. Thus, it is important to understand the basic mechanisms governing post-transcriptional control and how these processes can be co-opted to drive cancer cell phenotypes. In some cases, groups of mRNAs that encode protein involved in specific oncogenic processes can be co-regulated at multiple processing levels in order to turn on entire biochemical pathways. Indeed, the RNA regulon model was postulated as a means to understand how cells coordinately regulate transcripts encoding proteins in the same biochemical pathways. In this review, we describe some of the basic mRNA processes that are dysregulated in cancer and the biological impact this has on the cell. This dysregulation can affect networks of RNAs simultaneously thereby underpinning the oncogenic phenotypes observed.
Language	English
Publishing date	2018-11-05
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2606823-0
ISSN	1664-8021
ISSN	1664-8021
DOI	10.3389/fgene.2018.00512
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Article ; Online: The eukaryotic translation initiation factor eIF4E reprograms alternative splicing.

Ghram, Mehdi / Morris, Gavin / Culjkovic-Kraljacic, Biljana / Mars, Jean-Clement / Gendron, Patrick / Skrabanek, Lucy / Revuelta, Maria Victoria / Cerchietti, Leandro / Guzman, Monica L / Borden, Katherine L B

The EMBO journal

2023 Volume 42, Issue 7, Page(s) e110496

Abstract: Aberrant splicing is typically attributed to splice-factor (SF) mutation and contributes to malignancies including acute myeloid leukemia (AML). Here, we discovered a mutation-independent means to extensively reprogram alternative splicing (AS). We ... ...

Abstract	Aberrant splicing is typically attributed to splice-factor (SF) mutation and contributes to malignancies including acute myeloid leukemia (AML). Here, we discovered a mutation-independent means to extensively reprogram alternative splicing (AS). We showed that the dysregulated expression of eukaryotic translation initiation factor eIF4E elevated selective splice-factor production, thereby impacting multiple spliceosome complexes, including factors mutated in AML such as SF3B1 and U2AF1. These changes generated a splicing landscape that predominantly supported altered splice-site selection for ~800 transcripts in cell lines and ~4,600 transcripts in specimens from high-eIF4E AML patients otherwise harboring no known SF mutations. Nuclear RNA immunoprecipitations, export assays, polysome analyses, and mutational studies together revealed that eIF4E primarily increased SF production via its nuclear RNA export activity. By contrast, eIF4E dysregulation did not induce known SF mutations or alter spliceosome number. eIF4E interacted with the spliceosome and some pre-mRNAs, suggesting its direct involvement in specific splicing events. eIF4E induced simultaneous effects on numerous SF proteins, resulting in a much larger range of splicing alterations than in the case of mutation or dysregulation of individual SFs and providing a novel paradigm for splicing control and dysregulation.
MeSH term(s)	Humans ; Alternative Splicing ; RNA Splicing Factors/metabolism ; Eukaryotic Initiation Factor-4E/metabolism ; RNA Splicing ; Eukaryotic Initiation Factors/genetics ; Leukemia, Myeloid, Acute/genetics ; Mutation
Chemical Substances	RNA Splicing Factors ; Eukaryotic Initiation Factor-4E ; Eukaryotic Initiation Factors
Language	English
Publishing date	2023-02-27
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.2021110496
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Zs.A 1808: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 100: Show issues

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Article ; Online: Medicinal Chemistry and NMR Driven Discovery of Novel UDP-glucuronosyltransferase 1A Inhibitors That Overcome Therapeutic Resistance in Cells.

Osborne, Michael J / Sulekha, Anamika / Culjkovic-Kraljacic, Biljana / Gasiorek, Jadwiga / Ruediger, Edward / Jolicouer, Eric / Marinier, Anne / Assouline, Sarit / Borden, Katherine L B

Journal of molecular biology

2023 Volume 436, Issue 2, Page(s) 168378

Abstract: The UDP glucuronosyltransferases (UGT) deactivate many therapeutics via glucuronidation while being required for clearance of normal metabolites and xenobiotics. There are 19 UGT enzymes categorized into UGT1A and UGT2B families based on sequence ... ...

Abstract	The UDP glucuronosyltransferases (UGT) deactivate many therapeutics via glucuronidation while being required for clearance of normal metabolites and xenobiotics. There are 19 UGT enzymes categorized into UGT1A and UGT2B families based on sequence conservation. This presents a challenge in terms of targeting specific UGTs to overcome drug resistance without eliciting overt toxicity. Here, we identified for the first time that UGT1A4 is highly elevated in acute myeloid leukemia (AML) patients and its reduction corresponded to objective clinical responses. To develop inhibitors to UGT1A4, we leveraged previous NMR-based fragment screening data against the C-terminal domain of UGT1A (UGT1A-C). NMR and medicinal chemistry strategies identified novel chemical matter based on fragment compounds with the capacity to bind ∼20 fold more tightly to UGT1A-C (K
MeSH term(s)	Humans ; Catalytic Domain ; Chemistry, Pharmaceutical ; Drug Resistance, Neoplasm ; Glucuronosyltransferase/antagonists & inhibitors ; Uridine Diphosphate ; Drug Discovery ; Enzyme Inhibitors/chemistry ; Enzyme Inhibitors/pharmacology ; Magnetic Resonance Spectroscopy/methods
Chemical Substances	Glucuronosyltransferase (EC 2.4.1.17) ; Uridine Diphosphate (58-98-0) ; UGT1A1 enzyme (EC 2.4.1.-) ; Enzyme Inhibitors
Language	English
Publishing date	2023-12-01
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2023.168378
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Zs.A 867: Show issues

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Article ; Online: Molecular targeting of the UDP-glucuronosyltransferase enzymes in high-eukaryotic translation initiation factor 4E refractory/relapsed acute myeloid leukemia patients: a randomized phase II trial of vismodegib, ribavirin with or without decitabine.

Assouline, Sarit / Gasiorek, Jadwiga / Bergeron, Julie / Lambert, Caroline / Culjkovic-Kraljacic, Biljana / Cocolakis, Eftihia / Zakaria, Chadi / Szlachtycz, David / Yee, Karen / Borden, Katherine L B

Haematologica

2023 Volume 108, Issue 11, Page(s) 2946–2958

Abstract: Drug resistance underpins poor outcomes in many malignancies including refractory and relapsed acute myeloid leukemia (R/R AML). Glucuronidation is a common mechanism of drug inactivation impacting many AML therapies, e.g., cytarabine, decitabine, ... ...

Abstract	Drug resistance underpins poor outcomes in many malignancies including refractory and relapsed acute myeloid leukemia (R/R AML). Glucuronidation is a common mechanism of drug inactivation impacting many AML therapies, e.g., cytarabine, decitabine, azacytidine and venetoclax. In AML cells, the capacity for glucuronidation arises from increased production of the UDP-glucuronosyltransferase 1A (UGT1A) enzymes. UGT1A elevation was first observed in AML patients who relapsed after response to ribavirin, a drug used to target the eukaryotic translation initiation factor eIF4E, and subsequently in patients who relapsed on cytarabine. UGT1A elevation resulted from increased expression of the sonic-hedgehog transcription factor GLI1. Vismodegib inhibited GLI1, decreased UGT1A levels, reduced glucuronidation of ribavirin and cytarabine, and re-sensitized cells to these drugs. Here, we examined if UGT1A protein levels, and thus glucuronidation activity, were targetable in humans and if this corresponded to clinical response. We conducted a phase II trial using vismodegib with ribavirin, with or without decitabine, in largely heavily pre-treated patients with high-eIF4E AML. Pre-therapy molecular assessment of patients' blasts indicated highly elevated UGT1A levels relative to healthy volunteers. Among patients with partial response, blast response or prolonged stable disease, vismodegib reduced UGT1A levels, which corresponded to effective targeting of eIF4E by ribavirin. In all, our studies are the first to demonstrate that UGT1A protein, and thus glucuronidation, are targetable in humans. These studies pave the way for the development of therapies that impair glucuronidation, one of the most common drug deactivation modalities. Clinicaltrials.gov: NCT02073838.
MeSH term(s)	Humans ; Decitabine/therapeutic use ; Glucuronosyltransferase/metabolism ; Glucuronosyltransferase/therapeutic use ; Ribavirin/therapeutic use ; Ribavirin/metabolism ; Hedgehog Proteins/metabolism ; Hedgehog Proteins/therapeutic use ; Eukaryotic Initiation Factor-4E/metabolism ; Zinc Finger Protein GLI1/metabolism ; Zinc Finger Protein GLI1/therapeutic use ; Molecular Targeted Therapy ; Leukemia, Myeloid, Acute/drug therapy ; Leukemia, Myeloid, Acute/genetics ; Leukemia, Myeloid, Acute/metabolism ; Cytarabine ; Uridine Diphosphate/therapeutic use ; Antineoplastic Combined Chemotherapy Protocols/adverse effects
Chemical Substances	Decitabine (776B62CQ27) ; Glucuronosyltransferase (EC 2.4.1.17) ; HhAntag691 ; Ribavirin (49717AWG6K) ; Hedgehog Proteins ; Eukaryotic Initiation Factor-4E ; Zinc Finger Protein GLI1 ; Cytarabine (04079A1RDZ) ; Uridine Diphosphate (58-98-0)
Language	English
Publishing date	2023-11-01
Publishing country	Italy
Document type	Clinical Trial, Phase II ; Randomized Controlled Trial ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2333-4
ISSN	1592-8721 ; 0017-6567 ; 0390-6078
ISSN (online)	1592-8721
ISSN	0017-6567 ; 0390-6078
DOI	10.3324/haematol.2023.282791
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Uh III Zs.76: Show issues

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Article ; Online: Identification and Characterization of the Interaction Between the Methyl-7-Guanosine Cap Maturation Enzyme RNMT and the Cap-Binding Protein eIF4E.

Osborne, Michael J / Volpon, Laurent / Memarpoor-Yazdi, Mina / Pillay, Shubhadra / Thambipillai, Aksharh / Czarnota, Sylwia / Culjkovic-Kraljacic, Biljana / Trahan, Christian / Oeffinger, Marlene / Cowling, Victoria H / Borden, Katherine L B

Journal of molecular biology

2022 Volume 434, Issue 5, Page(s) 167451

Abstract: The control of RNA metabolism is an important aspect of molecular biology with wide-ranging impacts on cells. Central to processing of coding RNAs is the addition of the methyl-7 guanosine ( ... ...

Abstract	The control of RNA metabolism is an important aspect of molecular biology with wide-ranging impacts on cells. Central to processing of coding RNAs is the addition of the methyl-7 guanosine (m
MeSH term(s)	Eukaryotic Initiation Factor-4E/genetics ; Guanosine/metabolism ; Humans ; Methyltransferases/metabolism ; Protein Binding ; RNA Cap-Binding Proteins/genetics ; RNA Cap-Binding Proteins/metabolism ; RNA Caps/chemistry ; RNA Caps/genetics ; RNA Caps/metabolism
Chemical Substances	Eukaryotic Initiation Factor-4E ; RNA Cap-Binding Proteins ; RNA Caps ; Guanosine (12133JR80S) ; Methyltransferases (EC 2.1.1.-) ; mRNA (guanine(N7))-methyltransferase (EC 2.1.1.56)
Language	English
Publishing date	2022-01-10
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	80229-3
ISSN	1089-8638 ; 0022-2836
ISSN (online)	1089-8638
ISSN	0022-2836
DOI	10.1016/j.jmb.2022.167451
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Zs.A 867: Show issues

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Article ; Online: GLI1-Inducible Glucuronidation Targets a Broad Spectrum of Drugs.

Zahreddine, Hiba Ahmad / Culjkovic-Kraljacic, Biljana / Gasiorek, Jadwiga / Duchaine, Jean / Borden, Katherine L B

ACS chemical biology

2019 Volume 14, Issue 3, Page(s) 348–355

Abstract: Cancer therapies are plagued by resistance. Previously, we discovered a novel form of cancer drug resistance where the Glioma-associated protein 1 (GLI1) elevates UGT1A glucuronidation enzymes, thereby glucuronidating cytarabine and ribavirin, leading to ...

Abstract	Cancer therapies are plagued by resistance. Previously, we discovered a novel form of cancer drug resistance where the Glioma-associated protein 1 (GLI1) elevates UGT1A glucuronidation enzymes, thereby glucuronidating cytarabine and ribavirin, leading to resistance in leukemia patients. Here, we demonstrate that GLI1 imparts resistance to ∼40 compounds, including FDA-approved drugs with disparate chemotypes ( e.g., methotrexate and venetoclax). GLI1 indirectly elevates UGT1As via the chaperone calreticulin, which is required for resistance. Further, we demonstrate that resistant cells are more sensitive to ATP inhibitors, suggesting an Achilles' heel, which could be exploited in the future. In all, we identify GLI1-inducible glucuronidation as a broad-spectrum multidrug resistance pathway.
MeSH term(s)	Adenosine Triphosphate/antagonists & inhibitors ; Antimetabolites, Antineoplastic/chemistry ; Antimetabolites, Antineoplastic/metabolism ; Calreticulin/metabolism ; Cytarabine/chemistry ; Cytarabine/metabolism ; Drug Resistance, Multiple ; Drug Resistance, Neoplasm ; Drug Screening Assays, Antitumor ; Glucuronosyltransferase/metabolism ; Humans ; Small Molecule Libraries/chemistry ; Small Molecule Libraries/metabolism ; Zinc Finger Protein GLI1/antagonists & inhibitors
Chemical Substances	Antimetabolites, Antineoplastic ; Calreticulin ; Small Molecule Libraries ; Zinc Finger Protein GLI1 ; Cytarabine (04079A1RDZ) ; Adenosine Triphosphate (8L70Q75FXE) ; UGT1A1 enzyme (EC 2.4.1.-) ; Glucuronosyltransferase (EC 2.4.1.17)
Language	English
Publishing date	2019-02-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ISSN	1554-8937
ISSN (online)	1554-8937
DOI	10.1021/acschembio.8b01118
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Article: Sonic Hedgehog factor Gli1: As good as resistant.

Zahreddine, Hiba Ahmad / Culjkovic-Kraljacic, Biljana / Borden, Katherine Lb

Molecular & cellular oncology

2015 Volume 2, Issue 1, Page(s) e961827

Abstract: Chemoresistance remains a major impediment in cancer therapy. Although major progress has been made in understanding the mechanisms underlying resistance in cancer, there is still more to learn. Our studies provide evidence that Gli1 drives a novel form ... ...

Abstract	Chemoresistance remains a major impediment in cancer therapy. Although major progress has been made in understanding the mechanisms underlying resistance in cancer, there is still more to learn. Our studies provide evidence that Gli1 drives a novel form of drug resistance involving Phase II drug metabolism enzymes, specifically the UGT1A family.
Language	English
Publishing date	2015-02-24
Publishing country	United States
Document type	Journal Article
ISSN	2372-3556
ISSN	2372-3556
DOI	10.4161/23723548.2014.961827
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Article ; Online: The eukaryotic translation initiation factor eIF4E elevates steady-state m

Culjkovic-Kraljacic, Biljana / Skrabanek, Lucy / Revuelta, Maria V / Gasiorek, Jadwiga / Cowling, Victoria H / Cerchietti, Leandro / Borden, Katherine L B

Proceedings of the National Academy of Sciences of the United States of America

2020 Volume 117, Issue 43, Page(s) 26773–26783

Abstract: Methyl-7-guanosine ( ... ...

Abstract	Methyl-7-guanosine (m
MeSH term(s)	Cell Line, Tumor ; Eukaryotic Initiation Factor-4E/chemistry ; Eukaryotic Initiation Factor-4E/genetics ; Eukaryotic Initiation Factor-4E/metabolism ; Guanosine/analogs & derivatives ; Guanosine/chemistry ; Guanosine/genetics ; Guanosine/metabolism ; Humans ; Polyribosomes/metabolism ; RNA Caps/chemistry ; RNA Caps/genetics ; RNA Caps/metabolism ; RNA, Messenger/chemistry ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Transcriptome/genetics
Chemical Substances	8-methylguanosine ; Eukaryotic Initiation Factor-4E ; RNA Caps ; RNA, Messenger ; Guanosine (12133JR80S)
Language	English
Publishing date	2020-10-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2002360117
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