Historical Background
The serine-threonine kinase Pim-1 belongs to the Calmodulin-dependent protein kinase family together with two other highly conserved family members (Pim-2 and Pim-3). Pim-1 is the preferential site of integration for the Moloney murine leukemia virus (Proviral Integration for Moloney Virus) discovered over 25 years ago (Selten et al. 1985). Pim-1 plays pivotal roles in cellular proliferation, differentiation, metabolism, and survival by phosphorylating and interacting with many targets. A literature search reveals the dynamic expression and activity of Pim-1 depends upon cell type and response to stimuli, either pathologic or homeostatic. Specifically, Pim-1 is expressed in various hematopoietic sites including thymus, spleen, bone marrow, and fetal liver, but can also be found in the heart, oral epithelia, prostate, hippocampus, vascular smooth muscle, and many tumorigenic cell types...
This is a preview of subscription content, log in via an institution to check access.
References
Bachmann M, Moroy T. The serine/threonine kinase Pim-1. Int J Biochem Cell Biol. 2005;37(4):726–30.
Bachmann M, Kosan C, et al. The oncogenic serine/threonine kinase Pim-1 directly phosphorylates and activates the G2/M specific phosphatase Cdc25C. Int J Biochem Cell Biol. 2006;38(3):430–43.
Bhattacharya N, Wang Z, et al. Pim-1 associates with protein complexes necessary for mitosis. Chromosoma. 2002;111(2):80–95.
Borillo GA, Mason M, et al. Pim-1 kinase protects mitochondrial integrity in cardiomyocytes. Circ Res. 2010;106(7):1265–74.
Chen J, Kobayashi M, et al. Hypoxia-mediated up-regulation of Pim-1 contributes to solid tumor formation. Am J Pathol. 2009;175(1):400–11.
Cottage CT, Bailey B, et al. Cardiac progenitor cell cycling stimulated by Pim-1 kinase. Circ Res. 2010;106(5):891–901.
Fischer KM, Cottage CT, et al. Enhancement of myocardial regeneration through genetic engineering of cardiac progenitor cells expressing Pim-1 kinase. Circulation. 2009;120(21):2077–87.
Katare R, Caporali A, et al. Intravenous gene therapy with PIM-1 via a cardiotropic viral vector halts the progression of diabetic cardiomyopathy through promotion of prosurvival signaling. Circ Res. 2011;108(10):1238–51.
Krishnan N, Pan H, et al. Prolactin-regulated pim-1 transcription: identification of critical promoter elements and Akt signaling. Endocrine. 2003;20(1–2):123–30.
Mochizuki T, Kitanaka C, et al. Physical and functional interactions between Pim-1 kinase and Cdc25A phosphatase. Implications for the Pim-1-mediated activation of the c-Myc signaling pathway. J Biol Chem. 1999;274(26):18659–66.
Morishita D, Katayama R, et al. Pim kinases promote cell cycle progression by phosphorylating and down-regulating p27Kip1 at the transcriptional and posttranscriptional levels. Cancer Res. 2008;68(13):5076–85.
Muraski JA, Rota M, et al. Pim-1 regulates cardiomyocyte survival downstream of Akt. Nat Med. 2007;13(12):1467–75.
Nawijn MC, Alendar A, et al. For better or for worse: the role of Pim oncogenes in tumorigenesis. Nat Rev Cancer. 2011;11(1):23–34.
Selten G, Cuypers HT, et al. Proviral activation of the putative oncogene Pim-1 in MuLV induced T-cell lymphomas. EMBO J. 1985;4(7):1793–8.
Shay KP, Wang Z, et al. Pim-1 kinase stability is regulated by heat shock proteins and the ubiquitin-proteasome pathway. Mol Cancer Res. 2005;3(3):170–81.
Willert M, Augstein A, et al. Transcriptional regulation of Pim-1 kinase in vascular smooth muscle cells and its role for proliferation. Basic Res Cardiol. 2010;105(2):267–77.
Zhang Y, Wang Z, et al. Pim-1 kinase-dependent phosphorylation of p21Cip1/WAF1 regulates its stability and cellular localization in H1299 cells. Mol Cancer Res. 2007;5(9):909–22.
Zhang Y, Wang Z, et al. Pim kinase-dependent inhibition of c-Myc degradation. Oncogene. 2008;27(35):4809–19.
Zhao Y, Hamza MS, et al. Kruppel-like factor 5 modulates p53-independent apoptosis through Pim1 survival kinase in cancer cells. Oncogene. 2008;27(1):1–8.
Zippo A, De Robertis A, et al. PIM1-dependent phosphorylation of histone H3 at serine 10 is required for MYC-dependent transcriptional activation and oncogenic transformation. Nat Cell Biol. 2007;9(8):932–44.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2012 Springer Science+Business Media, LLC
About this entry
Cite this entry
Cottage, C.T., Sundararaman, B., Din, S., Hariharan, N., Sussman, M.A. (2012). Pim-1. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-0461-4_344
Download citation
DOI: https://doi.org/10.1007/978-1-4419-0461-4_344
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4419-0460-7
Online ISBN: 978-1-4419-0461-4
eBook Packages: Biomedical and Life SciencesReference Module Biomedical and Life Sciences