Activation of CAMK2 by pseudokinase PEAK1 represents a targetable pathway in triple negative breast cancer
The PEAK family of pseudokinases, comprising PEAK1-3, play oncogenic roles in several poor prognosis human cancers, including triple negative breast cancer (TNBC). However, therapeutic targeting of pseudokinases is challenging due to their lack of catalytic activity. To address this, we screen for P...
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| Veröffentlicht in: | Nature communications Jg. 16; H. 1; S. 1871 - 19 |
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22.02.2025
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| Abstract | The PEAK family of pseudokinases, comprising PEAK1-3, play oncogenic roles in several poor prognosis human cancers, including triple negative breast cancer (TNBC). However, therapeutic targeting of pseudokinases is challenging due to their lack of catalytic activity. To address this, we screen for PEAK1 effectors and identify calcium/calmodulin-dependent protein kinase 2 (CAMK2)D and CAMK2G. PEAK1 promotes CAMK2 activation in TNBC cells via PLCγ1/Ca
2+
signalling and direct binding to CAMK2. In turn, CAMK2 phosphorylates PEAK1 to enhance association with PEAK2, which is critical for PEAK1 oncogenic signalling. To achieve pharmacologic targeting of PEAK1/CAMK2, we repurpose RA306, a second generation CAMK2 inhibitor. RA306 inhibits PEAK1-enhanced migration and invasion of TNBC cells in vitro and significantly attenuates TNBC xenograft growth and metastasis in a manner mirrored by PEAK1 ablation. Overall, these studies establish PEAK1 as a critical cell signalling nexus that integrates Ca
2+
and tyrosine kinase signals and identify CAMK2 as a therapeutically ‘actionable’ target downstream of PEAK1.
The PEAK family of pseudokinases is known to play oncogenic roles in poor-prognosis triple negative breast cancer (TNBC). Here this group identifies the role of calcium/calmodulin-dependent protein kinase 2 (CAMK2) in targeting downstream of PEAK1 thereby utilizing RA306 (CAMK2 inhibitor) to effectively attenuate TNBC xenograft growth and block metastasis as well. |
|---|---|
| AbstractList | The PEAK family of pseudokinases, comprising PEAK1-3, play oncogenic roles in several poor prognosis human cancers, including triple negative breast cancer (TNBC). However, therapeutic targeting of pseudokinases is challenging due to their lack of catalytic activity. To address this, we screen for PEAK1 effectors and identify calcium/calmodulin-dependent protein kinase 2 (CAMK2)D and CAMK2G. PEAK1 promotes CAMK2 activation in TNBC cells via PLCγ1/Ca 2+ signalling and direct binding to CAMK2. In turn, CAMK2 phosphorylates PEAK1 to enhance association with PEAK2, which is critical for PEAK1 oncogenic signalling. To achieve pharmacologic targeting of PEAK1/CAMK2, we repurpose RA306, a second generation CAMK2 inhibitor. RA306 inhibits PEAK1-enhanced migration and invasion of TNBC cells in vitro and significantly attenuates TNBC xenograft growth and metastasis in a manner mirrored by PEAK1 ablation. Overall, these studies establish PEAK1 as a critical cell signalling nexus that integrates Ca 2+ and tyrosine kinase signals and identify CAMK2 as a therapeutically ‘actionable’ target downstream of PEAK1. The PEAK family of pseudokinases, comprising PEAK1-3, play oncogenic roles in several poor prognosis human cancers, including triple negative breast cancer (TNBC). However, therapeutic targeting of pseudokinases is challenging due to their lack of catalytic activity. To address this, we screen for PEAK1 effectors and identify calcium/calmodulin-dependent protein kinase 2 (CAMK2)D and CAMK2G. PEAK1 promotes CAMK2 activation in TNBC cells via PLCγ1/Ca2+ signalling and direct binding to CAMK2. In turn, CAMK2 phosphorylates PEAK1 to enhance association with PEAK2, which is critical for PEAK1 oncogenic signalling. To achieve pharmacologic targeting of PEAK1/CAMK2, we repurpose RA306, a second generation CAMK2 inhibitor. RA306 inhibits PEAK1-enhanced migration and invasion of TNBC cells in vitro and significantly attenuates TNBC xenograft growth and metastasis in a manner mirrored by PEAK1 ablation. Overall, these studies establish PEAK1 as a critical cell signalling nexus that integrates Ca2+ and tyrosine kinase signals and identify CAMK2 as a therapeutically ‘actionable’ target downstream of PEAK1. The PEAK family of pseudokinases is known to play oncogenic roles in poor-prognosis triple negative breast cancer (TNBC). Here this group identifies the role of calcium/calmodulin-dependent protein kinase 2 (CAMK2) in targeting downstream of PEAK1 thereby utilizing RA306 (CAMK2 inhibitor) to effectively attenuate TNBC xenograft growth and block metastasis as well. The PEAK family of pseudokinases, comprising PEAK1-3, play oncogenic roles in several poor prognosis human cancers, including triple negative breast cancer (TNBC). However, therapeutic targeting of pseudokinases is challenging due to their lack of catalytic activity. To address this, we screen for PEAK1 effectors and identify calcium/calmodulin-dependent protein kinase 2 (CAMK2)D and CAMK2G. PEAK1 promotes CAMK2 activation in TNBC cells via PLCγ1/Ca signalling and direct binding to CAMK2. In turn, CAMK2 phosphorylates PEAK1 to enhance association with PEAK2, which is critical for PEAK1 oncogenic signalling. To achieve pharmacologic targeting of PEAK1/CAMK2, we repurpose RA306, a second generation CAMK2 inhibitor. RA306 inhibits PEAK1-enhanced migration and invasion of TNBC cells in vitro and significantly attenuates TNBC xenograft growth and metastasis in a manner mirrored by PEAK1 ablation. Overall, these studies establish PEAK1 as a critical cell signalling nexus that integrates Ca and tyrosine kinase signals and identify CAMK2 as a therapeutically 'actionable' target downstream of PEAK1. The PEAK family of pseudokinases, comprising PEAK1-3, play oncogenic roles in several poor prognosis human cancers, including triple negative breast cancer (TNBC). However, therapeutic targeting of pseudokinases is challenging due to their lack of catalytic activity. To address this, we screen for PEAK1 effectors and identify calcium/calmodulin-dependent protein kinase 2 (CAMK2)D and CAMK2G. PEAK1 promotes CAMK2 activation in TNBC cells via PLCγ1/Ca 2+ signalling and direct binding to CAMK2. In turn, CAMK2 phosphorylates PEAK1 to enhance association with PEAK2, which is critical for PEAK1 oncogenic signalling. To achieve pharmacologic targeting of PEAK1/CAMK2, we repurpose RA306, a second generation CAMK2 inhibitor. RA306 inhibits PEAK1-enhanced migration and invasion of TNBC cells in vitro and significantly attenuates TNBC xenograft growth and metastasis in a manner mirrored by PEAK1 ablation. Overall, these studies establish PEAK1 as a critical cell signalling nexus that integrates Ca 2+ and tyrosine kinase signals and identify CAMK2 as a therapeutically ‘actionable’ target downstream of PEAK1. The PEAK family of pseudokinases is known to play oncogenic roles in poor-prognosis triple negative breast cancer (TNBC). Here this group identifies the role of calcium/calmodulin-dependent protein kinase 2 (CAMK2) in targeting downstream of PEAK1 thereby utilizing RA306 (CAMK2 inhibitor) to effectively attenuate TNBC xenograft growth and block metastasis as well. The PEAK family of pseudokinases, comprising PEAK1-3, play oncogenic roles in several poor prognosis human cancers, including triple negative breast cancer (TNBC). However, therapeutic targeting of pseudokinases is challenging due to their lack of catalytic activity. To address this, we screen for PEAK1 effectors and identify calcium/calmodulin-dependent protein kinase 2 (CAMK2)D and CAMK2G. PEAK1 promotes CAMK2 activation in TNBC cells via PLCγ1/Ca2+ signalling and direct binding to CAMK2. In turn, CAMK2 phosphorylates PEAK1 to enhance association with PEAK2, which is critical for PEAK1 oncogenic signalling. To achieve pharmacologic targeting of PEAK1/CAMK2, we repurpose RA306, a second generation CAMK2 inhibitor. RA306 inhibits PEAK1-enhanced migration and invasion of TNBC cells in vitro and significantly attenuates TNBC xenograft growth and metastasis in a manner mirrored by PEAK1 ablation. Overall, these studies establish PEAK1 as a critical cell signalling nexus that integrates Ca2+ and tyrosine kinase signals and identify CAMK2 as a therapeutically ‘actionable’ target downstream of PEAK1.The PEAK family of pseudokinases is known to play oncogenic roles in poor-prognosis triple negative breast cancer (TNBC). Here this group identifies the role of calcium/calmodulin-dependent protein kinase 2 (CAMK2) in targeting downstream of PEAK1 thereby utilizing RA306 (CAMK2 inhibitor) to effectively attenuate TNBC xenograft growth and block metastasis as well. The PEAK family of pseudokinases, comprising PEAK1-3, play oncogenic roles in several poor prognosis human cancers, including triple negative breast cancer (TNBC). However, therapeutic targeting of pseudokinases is challenging due to their lack of catalytic activity. To address this, we screen for PEAK1 effectors and identify calcium/calmodulin-dependent protein kinase 2 (CAMK2)D and CAMK2G. PEAK1 promotes CAMK2 activation in TNBC cells via PLCγ1/Ca2+ signalling and direct binding to CAMK2. In turn, CAMK2 phosphorylates PEAK1 to enhance association with PEAK2, which is critical for PEAK1 oncogenic signalling. To achieve pharmacologic targeting of PEAK1/CAMK2, we repurpose RA306, a second generation CAMK2 inhibitor. RA306 inhibits PEAK1-enhanced migration and invasion of TNBC cells in vitro and significantly attenuates TNBC xenograft growth and metastasis in a manner mirrored by PEAK1 ablation. Overall, these studies establish PEAK1 as a critical cell signalling nexus that integrates Ca2+ and tyrosine kinase signals and identify CAMK2 as a therapeutically 'actionable' target downstream of PEAK1.The PEAK family of pseudokinases, comprising PEAK1-3, play oncogenic roles in several poor prognosis human cancers, including triple negative breast cancer (TNBC). However, therapeutic targeting of pseudokinases is challenging due to their lack of catalytic activity. To address this, we screen for PEAK1 effectors and identify calcium/calmodulin-dependent protein kinase 2 (CAMK2)D and CAMK2G. PEAK1 promotes CAMK2 activation in TNBC cells via PLCγ1/Ca2+ signalling and direct binding to CAMK2. In turn, CAMK2 phosphorylates PEAK1 to enhance association with PEAK2, which is critical for PEAK1 oncogenic signalling. To achieve pharmacologic targeting of PEAK1/CAMK2, we repurpose RA306, a second generation CAMK2 inhibitor. RA306 inhibits PEAK1-enhanced migration and invasion of TNBC cells in vitro and significantly attenuates TNBC xenograft growth and metastasis in a manner mirrored by PEAK1 ablation. Overall, these studies establish PEAK1 as a critical cell signalling nexus that integrates Ca2+ and tyrosine kinase signals and identify CAMK2 as a therapeutically 'actionable' target downstream of PEAK1. Abstract The PEAK family of pseudokinases, comprising PEAK1-3, play oncogenic roles in several poor prognosis human cancers, including triple negative breast cancer (TNBC). However, therapeutic targeting of pseudokinases is challenging due to their lack of catalytic activity. To address this, we screen for PEAK1 effectors and identify calcium/calmodulin-dependent protein kinase 2 (CAMK2)D and CAMK2G. PEAK1 promotes CAMK2 activation in TNBC cells via PLCγ1/Ca2+ signalling and direct binding to CAMK2. In turn, CAMK2 phosphorylates PEAK1 to enhance association with PEAK2, which is critical for PEAK1 oncogenic signalling. To achieve pharmacologic targeting of PEAK1/CAMK2, we repurpose RA306, a second generation CAMK2 inhibitor. RA306 inhibits PEAK1-enhanced migration and invasion of TNBC cells in vitro and significantly attenuates TNBC xenograft growth and metastasis in a manner mirrored by PEAK1 ablation. Overall, these studies establish PEAK1 as a critical cell signalling nexus that integrates Ca2+ and tyrosine kinase signals and identify CAMK2 as a therapeutically ‘actionable’ target downstream of PEAK1. |
| ArticleNumber | 1871 |
| Author | Latham, Sharissa L. Ellisdon, Andrew M. Budnar, Srikanth Daly, Roger J. Bayly-Jones, Charles Nguyen, Lan K. Ma, Xiuquan Zhao, Tianyue Croucher, David R. Nguyen, Elizabeth V. Stratton, Margaret M. Cotton, Thomas R. Nguyen, Bao V. Clark, Kimberley C. Lim Kam Sian, Terry C. C. Yang, Xue Shin, Sung-Young Hu, Changyuan Chüeh, Anderly C. |
| Author_xml | – sequence: 1 givenname: Xue orcidid: 0000-0002-1016-5584 surname: Yang fullname: Yang, Xue organization: Cancer Program, Monash Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University – sequence: 2 givenname: Xiuquan orcidid: 0000-0001-7227-1289 surname: Ma fullname: Ma, Xiuquan organization: Cancer Program, Monash Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University – sequence: 3 givenname: Tianyue surname: Zhao fullname: Zhao, Tianyue organization: Cancer Program, Monash Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University – sequence: 4 givenname: David R. orcidid: 0000-0003-4965-8674 surname: Croucher fullname: Croucher, David R. organization: Garvan Institute of Medical Research, St Vincent’s Clinical School, Faculty of Medicine, UNSW Sydney – sequence: 5 givenname: Elizabeth V. surname: Nguyen fullname: Nguyen, Elizabeth V. organization: Cancer Program, Monash Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University – sequence: 6 givenname: Kimberley C. orcidid: 0000-0001-6277-8297 surname: Clark fullname: Clark, Kimberley C. organization: Cancer Program, Monash Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University – sequence: 7 givenname: Changyuan orcidid: 0000-0002-7193-1537 surname: Hu fullname: Hu, Changyuan organization: Cancer Program, Monash Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University – sequence: 8 givenname: Sharissa L. orcidid: 0000-0003-1128-5315 surname: Latham fullname: Latham, Sharissa L. organization: Garvan Institute of Medical Research, St Vincent’s Clinical School, Faculty of Medicine, UNSW Sydney – sequence: 9 givenname: Charles orcidid: 0000-0002-7573-7715 surname: Bayly-Jones fullname: Bayly-Jones, Charles organization: Cancer Program, Monash Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University – sequence: 10 givenname: Bao V. orcidid: 0000-0002-4693-3098 surname: Nguyen fullname: Nguyen, Bao V. organization: Department of Biochemistry and Molecular Biology, University of Massachusetts – sequence: 11 givenname: Srikanth orcidid: 0000-0002-8951-9081 surname: Budnar fullname: Budnar, Srikanth organization: Cancer Program, Monash Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University – sequence: 12 givenname: Sung-Young orcidid: 0000-0002-1447-9687 surname: Shin fullname: Shin, Sung-Young organization: Cancer Program, Monash Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University – sequence: 13 givenname: Lan K. orcidid: 0000-0003-4040-7705 surname: Nguyen fullname: Nguyen, Lan K. organization: Cancer Program, Monash Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University, South Australian Immunogenomics Cancer Institute, University of Adelaide – sequence: 14 givenname: Thomas R. orcidid: 0000-0001-6709-9218 surname: Cotton fullname: Cotton, Thomas R. organization: Cancer Program, Monash Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University – sequence: 15 givenname: Anderly C. orcidid: 0000-0003-1140-5516 surname: Chüeh fullname: Chüeh, Anderly C. organization: Cancer Program, Monash Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University – sequence: 16 givenname: Terry C. C. orcidid: 0000-0001-7038-1214 surname: Lim Kam Sian fullname: Lim Kam Sian, Terry C. C. organization: Cancer Program, Monash Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University – sequence: 17 givenname: Margaret M. orcidid: 0000-0003-2686-9022 surname: Stratton fullname: Stratton, Margaret M. organization: Department of Biochemistry and Molecular Biology, University of Massachusetts – sequence: 18 givenname: Andrew M. orcidid: 0000-0002-2248-9914 surname: Ellisdon fullname: Ellisdon, Andrew M. organization: Cancer Program, Monash Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University – sequence: 19 givenname: Roger J. orcidid: 0000-0002-5739-8027 surname: Daly fullname: Daly, Roger J. email: roger.daly@monash.edu organization: Cancer Program, Monash Biomedicine Discovery Institute, Department of Biochemistry and Molecular Biology, Monash University |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/39984440$$D View this record in MEDLINE/PubMed |
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| CitedBy_id | crossref_primary_10_1016_j_bcp_2025_117323 crossref_primary_10_1016_j_arr_2025_102886 |
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| Snippet | The PEAK family of pseudokinases, comprising PEAK1-3, play oncogenic roles in several poor prognosis human cancers, including triple negative breast cancer... Abstract The PEAK family of pseudokinases, comprising PEAK1-3, play oncogenic roles in several poor prognosis human cancers, including triple negative breast... |
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| SubjectTerms | 59 59/5 631/45/275 631/67/1347 631/67/395 631/80/86 82/58 82/80 96 96/1 96/106 96/95 Ablation Animals Breast cancer Ca2+/calmodulin-dependent protein kinase Calcium Calcium ions Calcium Signaling Calcium signalling Calcium-Calmodulin-Dependent Protein Kinase Type 2 - antagonists & inhibitors Calcium-Calmodulin-Dependent Protein Kinase Type 2 - genetics Calcium-Calmodulin-Dependent Protein Kinase Type 2 - metabolism Calmodulin Catalytic activity Cell activation Cell Line, Tumor Cell Movement - drug effects Female Humanities and Social Sciences Humans Kinases Metastases Metastasis Mice Mice, Nude multidisciplinary Phospholipase C gamma - metabolism Phosphorylation Prognosis Protein Kinase Inhibitors - pharmacology Proteins Science Science (multidisciplinary) Signal Transduction Therapeutic targets Triple Negative Breast Neoplasms - drug therapy Triple Negative Breast Neoplasms - genetics Triple Negative Breast Neoplasms - metabolism Triple Negative Breast Neoplasms - pathology Tyrosine Xenograft Model Antitumor Assays Xenografts Xenotransplantation |
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| Title | Activation of CAMK2 by pseudokinase PEAK1 represents a targetable pathway in triple negative breast cancer |
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