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Article ; Online: Direct and selective pharmacological disruption of the YAP-TEAD interface by IAG933 inhibits Hippo-dependent and RAS-MAPK-altered cancers.

Chapeau, Emilie A / Sansregret, Laurent / Galli, Giorgio G / Chène, Patrick / Wartmann, Markus / Mourikis, Thanos P / Jaaks, Patricia / Baltschukat, Sabrina / Barbosa, Ines A M / Bauer, Daniel / Brachmann, Saskia M / Delaunay, Clara / Estadieu, Claire / Faris, Jason E / Furet, Pascal / Harlfinger, Stefanie / Hueber, Andreas / Jiménez Núñez, Eloísa / Kodack, David P /

Mandon, Emeline / Martin, Typhaine / Mesrouze, Yannick / Romanet, Vincent / Scheufler, Clemens / Sellner, Holger / Stamm, Christelle / Sterker, Dario / Tordella, Luca / Hofmann, Francesco / Soldermann, Nicolas / Schmelzle, Tobias

Nature cancer

2024

Abstract: The YAP-TEAD protein-protein interaction mediates YAP oncogenic functions downstream of the Hippo pathway. To date, available YAP-TEAD pharmacologic agents bind into the lipid pocket of TEAD, targeting the interaction indirectly via allosteric changes. ... ...

Abstract	The YAP-TEAD protein-protein interaction mediates YAP oncogenic functions downstream of the Hippo pathway. To date, available YAP-TEAD pharmacologic agents bind into the lipid pocket of TEAD, targeting the interaction indirectly via allosteric changes. However, the consequences of a direct pharmacological disruption of the interface between YAP and TEADs remain largely unexplored. Here, we present IAG933 and its analogs as potent first-in-class and selective disruptors of the YAP-TEAD protein-protein interaction with suitable properties to enter clinical trials. Pharmacologic abrogation of the interaction with all four TEAD paralogs resulted in YAP eviction from chromatin and reduced Hippo-mediated transcription and induction of cell death. In vivo, deep tumor regression was observed in Hippo-driven mesothelioma xenografts at tolerated doses in animal models as well as in Hippo-altered cancer models outside mesothelioma. Importantly this also extended to larger tumor indications, such as lung, pancreatic and colorectal cancer, in combination with RTK, KRAS-mutant selective and MAPK inhibitors, leading to more efficacious and durable responses. Clinical evaluation of IAG933 is underway.
Language	English
Publishing date	2024-04-02
Publishing country	England
Document type	Journal Article
ISSN	2662-1347
ISSN (online)	2662-1347
DOI	10.1038/s43018-024-00754-9
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Cancer lineage-specific regulation of YAP responsive elements revealed through large-scale functional epigenomic screens.

Nature communications

2023 Volume 14, Issue 1, Page(s) 3907

Abstract: YAP is a key transcriptional co-activator of TEADs, it regulates cell growth and is frequently activated in cancer. In Malignant Pleural Mesothelioma (MPM), YAP is activated by loss-of-function mutations in upstream components of the Hippo pathway, while, ...

Abstract	YAP is a key transcriptional co-activator of TEADs, it regulates cell growth and is frequently activated in cancer. In Malignant Pleural Mesothelioma (MPM), YAP is activated by loss-of-function mutations in upstream components of the Hippo pathway, while, in Uveal Melanoma (UM), YAP is activated in a Hippo-independent manner. To date, it is unclear if and how the different oncogenic lesions activating YAP impact its oncogenic program, which is particularly relevant for designing selective anti-cancer therapies. Here we show that, despite YAP being essential in both MPM and UM, its interaction with TEAD is unexpectedly dispensable in UM, limiting the applicability of TEAD inhibitors in this cancer type. Systematic functional interrogation of YAP regulatory elements in both cancer types reveals convergent regulation of broad oncogenic drivers in both MPM and UM, but also strikingly selective programs. Our work reveals unanticipated lineage-specific features of the YAP regulatory network that provide important insights to guide the design of tailored therapeutic strategies to inhibit YAP signaling across different cancer types.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; YAP-Signaling Proteins ; Epigenomics ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Signal Transduction/genetics ; Neoplasms
Chemical Substances	Adaptor Proteins, Signal Transducing ; YAP-Signaling Proteins ; Transcription Factors
Language	English
Publishing date	2023-07-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-39527-w
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Article ; Online: CRISPR Screening Identifies Mechanisms of Resistance to KRASG12C and SHP2 Inhibitor Combinations in Non-Small Cell Lung Cancer.

Cancer research

2023 Volume 83, Issue 24, Page(s) 4130–4141

Abstract: Although KRASG12C inhibitors show clinical activity in patients with KRAS G12C mutated non-small cell lung cancer (NSCLC) and other solid tumor malignancies, response is limited by multiple mechanisms of resistance. The KRASG12C inhibitor JDQ443 shows ... ...

Abstract	Although KRASG12C inhibitors show clinical activity in patients with KRAS G12C mutated non-small cell lung cancer (NSCLC) and other solid tumor malignancies, response is limited by multiple mechanisms of resistance. The KRASG12C inhibitor JDQ443 shows enhanced preclinical antitumor activity combined with the SHP2 inhibitor TNO155, and the combination is currently under clinical evaluation. To identify rational combination strategies that could help overcome or prevent some types of resistance, we evaluated the duration of tumor responses to JDQ443 ± TNO155, alone or combined with the PI3Kα inhibitor alpelisib and/or the cyclin-dependent kinase 4/6 inhibitor ribociclib, in xenograft models derived from a KRASG12C-mutant NSCLC line and investigated the genetic mechanisms associated with loss of response to combined KRASG12C/SHP2 inhibition. Tumor regression by single-agent JDQ443 at clinically relevant doses lasted on average 2 weeks and was increasingly extended by the double, triple, or quadruple combinations. Growth resumption was accompanied by progressively increased KRAS G12C amplification. Functional genome-wide CRISPR screening in KRASG12C-dependent NSCLC lines with distinct mutational profiles to identify adaptive mechanisms of resistance revealed sensitizing and rescuing genetic interactions with KRASG12C/SHP2 coinhibition; FGFR1 loss was the strongest sensitizer, and PTEN loss the strongest rescuer. Consistently, the antiproliferative activity of KRASG12C/SHP2 inhibition was strongly enhanced by PI3K inhibitors. Overall, KRAS G12C amplification and alterations of the MAPK/PI3K pathway were predominant mechanisms of resistance to combined KRASG12C/SHP2 inhibitors in preclinical settings. The biological nodes identified by CRISPR screening might provide additional starting points for effective combination treatments. Significance: Identification of resistance mechanisms to KRASG12C/SHP2 coinhibition highlights the need for additional combination therapies for lung cancer beyond on-pathway combinations and offers the basis for development of more effective combination approaches. See related commentary by Johnson and Haigis, p. 4005.
MeSH term(s)	Humans ; Carcinoma, Non-Small-Cell Lung/drug therapy ; Carcinoma, Non-Small-Cell Lung/genetics ; Carcinoma, Non-Small-Cell Lung/pathology ; Lung Neoplasms/drug therapy ; Lung Neoplasms/genetics ; Lung Neoplasms/pathology ; Phosphatidylinositol 3-Kinases/genetics ; Clustered Regularly Interspaced Short Palindromic Repeats ; Proto-Oncogene Proteins p21(ras)/genetics ; Protein Kinase Inhibitors/pharmacology ; Protein Kinase Inhibitors/therapeutic use ; Early Detection of Cancer ; Enzyme Inhibitors/therapeutic use ; Mutation ; Cell Line, Tumor
Chemical Substances	Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; JDQ443 ; Proto-Oncogene Proteins p21(ras) (EC 3.6.5.2) ; Protein Kinase Inhibitors ; Enzyme Inhibitors
Language	English
Publishing date	2023-11-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1432-1
ISSN	1538-7445 ; 0008-5472
ISSN (online)	1538-7445
ISSN	0008-5472
DOI	10.1158/0008-5472.CAN-23-1127
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Article ; Online: Therapeutic Assessment of Targeting ASNS Combined with l-Asparaginase Treatment in Solid Tumors and Investigation of Resistance Mechanisms.

Apfel, Verena / Begue, Damien / Cordo', Valentina / Holzer, Laura / Martinuzzi, Laetitia / Buhles, Alexandra / Kerr, Grainne / Barbosa, Ines / Naumann, Ulrike / Piquet, Michelle / Ruddy, David / Weiss, Andreas / Ferretti, Stephane / Almeida, Reinaldo / Bonenfant, Debora / Tordella, Luca / Galli, Giorgio G

ACS pharmacology & translational science

2021 Volume 4, Issue 1, Page(s) 327–337

Abstract: Asparagine deprivation by l-asparaginase (L-ASNase) is an effective therapeutic strategy in acute lymphoblastic leukemia, with resistance occurring due to upregulation of ASNS, the only human enzyme synthetizing asparagine ( ...

Abstract	Asparagine deprivation by l-asparaginase (L-ASNase) is an effective therapeutic strategy in acute lymphoblastic leukemia, with resistance occurring due to upregulation of ASNS, the only human enzyme synthetizing asparagine (
Language	English
Publishing date	2021-01-13
Publishing country	United States
Document type	Journal Article
ISSN	2575-9108
ISSN (online)	2575-9108
DOI	10.1021/acsptsci.0c00196
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Article ; Online: Cancer lineage-specific regulation of YAP responsive elements revealed through large-scale functional epigenomic screens

Nature Communications, Vol 14, Iss 1, Pp 1-

2023 Volume 15

Abstract: Abstract YAP is a key transcriptional co-activator of TEADs, it regulates cell growth and is frequently activated in cancer. In Malignant Pleural Mesothelioma (MPM), YAP is activated by loss-of-function mutations in upstream components of the Hippo ... ...

Abstract	Abstract YAP is a key transcriptional co-activator of TEADs, it regulates cell growth and is frequently activated in cancer. In Malignant Pleural Mesothelioma (MPM), YAP is activated by loss-of-function mutations in upstream components of the Hippo pathway, while, in Uveal Melanoma (UM), YAP is activated in a Hippo-independent manner. To date, it is unclear if and how the different oncogenic lesions activating YAP impact its oncogenic program, which is particularly relevant for designing selective anti-cancer therapies. Here we show that, despite YAP being essential in both MPM and UM, its interaction with TEAD is unexpectedly dispensable in UM, limiting the applicability of TEAD inhibitors in this cancer type. Systematic functional interrogation of YAP regulatory elements in both cancer types reveals convergent regulation of broad oncogenic drivers in both MPM and UM, but also strikingly selective programs. Our work reveals unanticipated lineage-specific features of the YAP regulatory network that provide important insights to guide the design of tailored therapeutic strategies to inhibit YAP signaling across different cancer types.
Keywords	Science ; Q
Language	English
Publishing date	2023-07-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Structure of the MRAS-SHOC2-PP1C phosphatase complex.

Nature

2022 Volume 609, Issue 7926, Page(s) 416–423

Abstract: RAS-MAPK signalling is fundamental for cell proliferation and is altered in most human ... ...

Abstract	RAS-MAPK signalling is fundamental for cell proliferation and is altered in most human cancers
MeSH term(s)	14-3-3 Proteins ; Crystallography, X-Ray ; Guanosine Triphosphate/metabolism ; Humans ; Intracellular Signaling Peptides and Proteins/chemistry ; Intracellular Signaling Peptides and Proteins/metabolism ; MAP Kinase Signaling System ; Multiprotein Complexes/chemistry ; Mutation ; Protein Isoforms/chemistry ; Protein Isoforms/metabolism ; Protein Phosphatase 1/chemistry ; Protein Phosphatase 1/genetics ; Protein Phosphatase 1/metabolism ; Protein Subunits/chemistry ; Protein Subunits/metabolism ; raf Kinases ; ras Proteins/chemistry ; ras Proteins/metabolism
Chemical Substances	14-3-3 Proteins ; Intracellular Signaling Peptides and Proteins ; MRAS protein, human ; Multiprotein Complexes ; Protein Isoforms ; Protein Subunits ; SHOC2 protein, human ; Guanosine Triphosphate (86-01-1) ; raf Kinases (EC 2.7.11.1) ; Protein Phosphatase 1 (EC 3.1.3.16) ; ras Proteins (EC 3.6.5.2)
Language	English
Publishing date	2022-07-13
Publishing country	England
Document type	Journal Article
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-022-05086-1
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Zs.A 26: 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 9: Show issues
Zs.MO 244: Show issues

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Article ; Online: DCAF1-based PROTACs with activity against clinically validated targets overcoming intrinsic- and acquired-degrader resistance.

Schröder, Martin / Renatus, Martin / Liang, Xiaoyou / Meili, Fabian / Zoller, Thomas / Ferrand, Sandrine / Gauter, Francois / Li, Xiaoyan / Sigoillot, Frederic / Gleim, Scott / Stachyra, Therese-Marie / Thomas, Jason R / Begue, Damien / Khoshouei, Maryam / Lefeuvre, Peggy / Andraos-Rey, Rita / Chung, BoYee / Ma, Renate / Pinch, Benika /

Nature communications

2024 Volume 15, Issue 1, Page(s) 275

Abstract: Targeted protein degradation (TPD) mediates protein level through small molecule induced redirection of E3 ligases to ubiquitinate neo-substrates and mark them for proteasomal degradation. TPD has recently emerged as a key modality in drug discovery. So ... ...

Abstract	Targeted protein degradation (TPD) mediates protein level through small molecule induced redirection of E3 ligases to ubiquitinate neo-substrates and mark them for proteasomal degradation. TPD has recently emerged as a key modality in drug discovery. So far only a few ligases have been utilized for TPD. Interestingly, the workhorse ligase CRBN has been observed to be downregulated in settings of resistance to immunomodulatory inhibitory drugs (IMiDs). Here we show that the essential E3 ligase receptor DCAF1 can be harnessed for TPD utilizing a selective, non-covalent DCAF1 binder. We confirm that this binder can be functionalized into an efficient DCAF1-BRD9 PROTAC. Chemical and genetic rescue experiments validate specific degradation via the CRL4
MeSH term(s)	Carrier Proteins/metabolism ; Proteolysis ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Proteolysis Targeting Chimera
Chemical Substances	Carrier Proteins ; Ubiquitin ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; Proteolysis Targeting Chimera
Language	English
Publishing date	2024-01-04
Publishing country	England
Document type	Journal Article
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-44237-4
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Article ; Online: DCAF1-based PROTACs with activity against clinically validated targets overcoming intrinsic- and acquired-degrader resistance

Martin Schröder / Martin Renatus / Xiaoyou Liang / Fabian Meili / Thomas Zoller / Sandrine Ferrand / Francois Gauter / Xiaoyan Li / Frederic Sigoillot / Scott Gleim / Therese-Marie Stachyra / Jason R. Thomas / Damien Begue / Maryam Khoshouei / Peggy Lefeuvre / Rita Andraos-Rey / BoYee Chung / Renate Ma / Benika Pinch /

Nature Communications, Vol 15, Iss 1, Pp 1-

2024 Volume 19

Abstract: Abstract Targeted protein degradation (TPD) mediates protein level through small molecule induced redirection of E3 ligases to ubiquitinate neo-substrates and mark them for proteasomal degradation. TPD has recently emerged as a key modality in drug ... ...

Abstract	Abstract Targeted protein degradation (TPD) mediates protein level through small molecule induced redirection of E3 ligases to ubiquitinate neo-substrates and mark them for proteasomal degradation. TPD has recently emerged as a key modality in drug discovery. So far only a few ligases have been utilized for TPD. Interestingly, the workhorse ligase CRBN has been observed to be downregulated in settings of resistance to immunomodulatory inhibitory drugs (IMiDs). Here we show that the essential E3 ligase receptor DCAF1 can be harnessed for TPD utilizing a selective, non-covalent DCAF1 binder. We confirm that this binder can be functionalized into an efficient DCAF1-BRD9 PROTAC. Chemical and genetic rescue experiments validate specific degradation via the CRL4DCAF1 E3 ligase. Additionally, a dasatinib-based DCAF1 PROTAC successfully degrades cytosolic and membrane-bound tyrosine kinases. A potent and selective DCAF1-BTK-PROTAC (DBt-10) degrades BTK in cells with acquired resistance to CRBN-BTK-PROTACs while the DCAF1-BRD9 PROTAC (DBr-1) provides an alternative strategy to tackle intrinsic resistance to VHL-degrader, highlighting DCAF1-PROTACS as a promising strategy to overcome ligase mediated resistance in clinical settings.
Keywords	Science ; Q
Subject code	571
Language	English
Publishing date	2024-01-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: PAX8 activates metabolic genes via enhancer elements in Renal Cell Carcinoma.

Bleu, Melusine / Gaulis, Swann / Lopes, Rui / Sprouffske, Kathleen / Apfel, Verena / Holwerda, Sjoerd / Pregnolato, Marco / Yildiz, Umut / Cordoʹ, Valentina / Dost, Antonella F M / Knehr, Judith / Carbone, Walter / Lohmann, Felix / Lin, Charles Y / Bradner, James E / Kauffmann, Audrey / Tordella, Luca / Roma, Guglielmo / Galli, Giorgio G

Nature communications

2019 Volume 10, Issue 1, Page(s) 3739

Abstract: Transcription factor networks shape the gene expression programs responsible for normal cell identity and pathogenic state. Using Core Regulatory Circuitry analysis (CRC), we identify PAX8 as a candidate oncogene in Renal Cell Carcinoma (RCC) cells. ... ...

Abstract	Transcription factor networks shape the gene expression programs responsible for normal cell identity and pathogenic state. Using Core Regulatory Circuitry analysis (CRC), we identify PAX8 as a candidate oncogene in Renal Cell Carcinoma (RCC) cells. Validation of large-scale functional genomic screens confirms that PAX8 silencing leads to decreased proliferation of RCC cell lines. Epigenomic analyses of PAX8-dependent cistrome demonstrate that PAX8 largely occupies active enhancer elements controlling genes involved in various metabolic pathways. We selected the ferroxidase Ceruloplasmin (CP) as an exemplary gene to dissect PAX8 molecular functions. PAX8 recruits histone acetylation activity at bound enhancers looping onto the CP promoter. Importantly, CP expression correlates with sensitivity to PAX8 silencing and identifies a subset of RCC cases with poor survival. Our data identifies PAX8 as a candidate oncogene in RCC and provides a potential biomarker to monitor its activity.
MeSH term(s)	Acetylation ; Biomarkers, Tumor/genetics ; Carcinoma, Renal Cell/genetics ; Cell Line, Tumor ; Cell Proliferation/genetics ; Ceruloplasmin/genetics ; Ceruloplasmin/metabolism ; Enhancer Elements, Genetic/genetics ; Gene Expression Regulation, Neoplastic/genetics ; Histones/metabolism ; Humans ; Kidney Neoplasms/genetics ; PAX8 Transcription Factor/genetics ; Promoter Regions, Genetic/genetics ; RNA Interference ; RNA, Small Interfering/genetics
Chemical Substances	Biomarkers, Tumor ; Histones ; PAX8 Transcription Factor ; PAX8 protein, human ; RNA, Small Interfering ; Ceruloplasmin (EC 1.16.3.1)
Language	English
Publishing date	2019-08-20
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-019-11672-1
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Article ; Online: PAX8 activates metabolic genes via enhancer elements in Renal Cell Carcinoma

Melusine Bleu / Swann Gaulis / Rui Lopes / Kathleen Sprouffske / Verena Apfel / Sjoerd Holwerda / Marco Pregnolato / Umut Yildiz / Valentina Cordoʹ / Antonella F. M. Dost / Judith Knehr / Walter Carbone / Felix Lohmann / Charles Y. Lin / James E. Bradner / Audrey Kauffmann / Luca Tordella / Guglielmo Roma / Giorgio G. Galli

Nature Communications, Vol 10, Iss 1, Pp 1-

2019 Volume 10

Abstract: Transcription factors are critical regulators of cell identity. Here, the authors use computational and functional genomic approaches to show an oncogenic role of PAX8 in renal cancer. Mechanistic dissection of PAX8 functions reveal its role in ... ...

Abstract	Transcription factors are critical regulators of cell identity. Here, the authors use computational and functional genomic approaches to show an oncogenic role of PAX8 in renal cancer. Mechanistic dissection of PAX8 functions reveal its role in activating genes associated with metabolic pathways.
Keywords	Science ; Q
Language	English
Publishing date	2019-08-01T00:00:00Z
Publisher	Nature Publishing Group
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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