Journal of Advances in Molecular Biology
CaM Kinase I Regulation of p53 in Breast Cancer Cells
Download PDF (2973.1 KB) PP. 7 - 23 Pub. Date: June 1, 2020
Author(s)
- Renee C. Geck
The Biology Department, George Fox University, 414 N. Meridian St, Newberg, OR 97132, United States - Cody Coblentz
The Biology Department, George Fox University, 414 N. Meridian St, Newberg, OR 97132, United States - Angela Rofelty
The Biology Department, George Fox University, 414 N. Meridian St, Newberg, OR 97132, United States - John M. Schmitt*
The Biology Department, George Fox University, 414 N. Meridian St, Newberg, OR 97132, United States
Abstract
Keywords
References
[1] Brzozowski, J.S. and K.A. Skelding, The Multi-Functional Calcium/Calmodulin Stimulated Protein Kinase (CaMK) Family: Emerging Targets for Anti-Cancer Therapeutic Intervention. Pharmaceuticals (Basel), 2019. 12(1).
[2] Simon, B., A.S. Huart, and M. Wilmanns, Molecular mechanisms of protein kinase regulation by calcium/calmodulin. Bioorg Med Chem, 2015. 23(12): p. 2749-60.
[3] Takemoto-Kimura, S., et al., Calmodulin kinases: essential regulators in health and disease. J Neurochem, 2017. 141(6): p. 808-818.
[4] Bayer, K.U. and H. Schulman, CaM Kinase: Still Inspiring at 40. Neuron, 2019. 103(3): p. 380-394.
[5] Schmitt, J.M., et al., Calcium activation of ERK mediated by calmodulin kinase I. J Biol Chem, 2004. 279(23): p. 24064-72.
[6] Schmitt, J.M., et al., Calmodulin-dependent kinase kinase/calmodulin kinase I activity gates extracellularregulated kinase-dependent long-term potentiation. J Neurosci, 2005. 25(5): p. 1281-90.
[7] Schmitt, J.M., et al., ERK activation and cell growth require CaM kinases in MCF-7 breast cancer cells. Mol Cell Biochem, 2010. 335(1-2): p. 155-71.
[8] Kahl, C.R. and A.R. Means, Regulation of cyclin D1/Cdk4 complexes by calcium/calmodulin-dependent protein kinase I. J Biol Chem, 2004. 279(15): p. 15411-9.
[9] Lu, F., et al., Downregulation of CREB Promotes Cell Proliferation by Mediating G1/S Phase Transition in Hodgkin Lymphoma. Oncol Res, 2016. 24(3): p. 171-9.
[10] Sethi, S., et al., Social Context Enhances Hormonal Modulation of Pheromone Detection in Drosophila. Curr Biol, 2019. 29(22): p. 3887-3898 e4.
[11] Mallampalli, R.K., et al., Fbxl12 triggers G1 arrest by mediating degradation of calmodulin kinase I. Cell Signal, 2013.
[12] Kang, X., et al., CAMKs support development of acute myeloid leukemia. J Hematol Oncol, 2018. 11(1): p. 30.
[13] Davare, M.A., T. Saneyoshi, and T.R. Soderling, Calmodulin-kinases regulate basal and estrogen stimulated medulloblastoma migration via Rac1. J Neurooncol, 2011. 104(1): p. 65-82.
[14] Jadeja, R.N., et al., M3 muscarinic receptor activation reduces hepatocyte lipid accumulation via CaMKKbeta/AMPK pathway. Biochem Pharmacol, 2019. 169: p. 113613.
[15] Penfold, L., et al., CAMKK2 Promotes Prostate Cancer Independently of AMPK via Increased Lipogenesis. Cancer Res, 2018. 78(24): p. 6747-6761.
[16] Tokumitsu, H., et al., A single amino acid difference between alpha and beta Ca2+/calmodulin-dependent protein kinase kinase dictates sensitivity to the specific inhibitor, STO-609. J Biol Chem, 2003. 278(13): p. 10908-13.
[17] Rodriguez-Mora, O.G., et al., Calcium/calmodulin-dependent kinase I and calcium/calmodulin-dependent kinase kinase participate in the control of cell cycle progression in MCF-7 human breast cancer cells. Cancer Res, 2005. 65(12): p. 5408-16.
[18] Brufsky, A.M. and M.N. Dickler, Estrogen Receptor-Positive Breast Cancer: Exploiting Signaling Pathways Implicated in Endocrine Resistance. Oncologist, 2018. 23(5): p. 528-539.
[19] Jameera Begam, A., S. Jubie, and M.J. Nanjan, Estrogen receptor agonists/antagonists in breast cancer therapy: A critical review. Bioorg Chem, 2017. 71: p. 257-274.
[20] Improta-Brears, T., et al., Estrogen-induced activation of mitogen-activated protein kinase requires mobilization of intracellular calcium. Proc Natl Acad Sci U S A, 1999. 96(8): p. 4686-91.
[21] Pedram, A., et al., Developmental phenotype of a membrane only estrogen receptor alpha (MOER) mouse. J Biol Chem, 2009. 284(6): p. 3488-95.
[22] Bertheau, P., et al., p53 in breast cancer subtypes and new insights into response to chemotherapy. Breast, 2013. 22 Suppl 2: p. S27-9.
[23] Meek, D.W., Regulation of the p53 response and its relationship to cancer. Biochem J, 2015. 469(3): p. 325-46.
[24] Chen, J., The Cell-Cycle Arrest and Apoptotic Functions of p53 in Tumor Initiation and Progression. Cold Spring Harb Perspect Med, 2016. 6(3): p. a026104.
[25] Vousden, K.H. and C. Prives, Blinded by the Light: The Growing Complexity of p53. Cell, 2009. 137(3): p. 413- 31.
[26] Qu, L., et al., Endoplasmic reticulum stress induces p53 cytoplasmic localization and prevents p53-dependent apoptosis by a pathway involving glycogen synthase kinase-3beta. Genes Dev, 2004. 18(3): p. 261-77.
[27] Yogosawa, S. and K. Yoshida, Tumor suppressive role for kinases phosphorylating p53 in DNA damage-induced apoptosis. Cancer Sci, 2018. 109(11): p. 3376-3382.
[28] Rajagopalan, S., et al., 14-3-3 activation of DNA binding of p53 by enhancing its association into tetramers. Nucleic Acids Res, 2008. 36(18): p. 5983-91.
[29] Schmitt, J.M., et al., Estrogen Activation of CaM Kinases and Transcription Is Blocked by Vitamin D in MCF- 7 Breast Cancer Cells. Journal of Advances in Molecular Biology, 2017. 1(3): p. 129-147.
[30] Schmitt, J.M., et al., CaM kinase control of AKT and LNCaP cell survival. J Cell Biochem, 2012. 113(5): p. 1514-26.
[31] Gocher, A.M., et al., Akt activation by Ca(2+)/calmodulin-dependent protein kinase kinase 2 (CaMKK2) in ovarian cancer cells. J Biol Chem, 2017. 292(34): p. 14188-14204.
[32] Zhang, X., M.R. Diaz, and D. Yee, Fulvestrant regulates epidermal growth factor (EGF) family ligands to activate EGF receptor (EGFR) signaling in breast cancer cells. 2013. 139(2): p. 351-360.
[33] Chi, M., et al., Phosphorylation of calcium/calmodulin-stimulated protein kinase II at T286 enhances invasion and migration of human breast cancer cells. Sci Rep, 2016. 6: p. 33132.
[34] Foster, J.S., et al., Estrogens down-regulate p27Kip1 in breast cancer cells through Skp2 and through nuclear export mediated by the ERK pathway. J Biol Chem, 2003. 278(42): p. 41355-66.
[35] Fredersdorf, S., et al., High level expression of p27(kip1) and cyclin D1 in some human breast cancer cells: inverse correlation between the expression of p27(kip1) and degree of malignancy in human breast and colorectal cancers. Proc Natl Acad Sci U S A, 1997. 94(12): p. 6380-5.
[36] Li, W., et al., A truncated p53 in human lung cancer cells as a critical determinant of proliferation and invasiveness. Tumor Biology, 2017. 39(6): p. 101042831770382.
[37] Komarov, P.G., et al., A chemical inhibitor of p53 that protects mice from the side effects of cancer therapy. Science, 1999. 285(5434): p. 1733-7.
[38] Li, Q., et al., Genetic analysis of p53 nuclear importation. Oncogene, 2007. 26(57): p. 7885-93.
[39] Liang, S.H. and M.F. Clarke, A bipartite nuclear localization signal is required for p53 nuclear import regulated by a carboxyl-terminal domain. J Biol Chem, 1999. 274(46): p. 32699-703.
[40] Liang, S.H. and M.F. Clarke, The nuclear import of p53 is determined by the presence of a basic domain and its relative position to the nuclear localization signal. Oncogene, 1999. 18(12): p. 2163-6.
[41] Lin, F., et al., GTSE1 is involved in breast cancer progression in p53 mutation-dependent manner. Journal of Experimental & Clinical Cancer Research, 2019. 38(1).
[42] Korkmaz, G., et al., A CRISPR-Cas9 screen identifies essential CTCF anchor sites for estrogen receptor-driven breast cancer cell proliferation. Nucleic Acids Research, 2019. 47(18): p. 9557-9572.
[43] Bailey, S.T., et al., Estrogen receptor prevents p53-dependent apoptosis in breast cancer. Proc Natl Acad Sci U S A, 2012. 109(44): p. 18060-5.
[44] Ou, Y.H., et al., p53 C-terminal phosphorylation by CHK1 and CHK2 participates in the regulation of DNAdamage- induced C-terminal acetylation. Mol Biol Cell, 2005. 16(4): p. 1684-95.
[45] Rajagopalan, S., et al., Mechanistic differences in the transcriptional activation of p53 by 14-3-3 isoforms. Nucleic Acids Res, 2010. 38(3): p. 893-906.
[46] van Dieck, J., et al., Posttranslational modifications affect the interaction of S100 proteins with tumor suppressor p53. J Mol Biol, 2009. 394(5): p. 922-30.
[47] Mueller, A., et al., The calcium-binding protein S100A2 interacts with p53 and modulates its transcriptional activity. J Biol Chem, 2005. 280(32): p. 29186-93.