Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Gene Review:

Pim2 - proviral integration site 2

Mus musculus

Synonyms: DXCch3, Pim-2, Serine/threonine-protein kinase pim-2

Hammerman, P.S. et al., Konietzko, U. et al., Lesley, R. et al., Fox, C.J. et al., Macdonald, A. et al., et al.

Macdonald, Campbell, Toth, McLauchlan, Hastie, Arthur,

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Disease relevance of Pim2

Over-expression of Pim-1 and Pim-2 in mice promotes the development of lymphomas, and up-regulation of Pim expression has been observed in several human cancers [1].

High impact information on Pim2

Pim-2-dependent maintenance of cell size and survival correlated with its ability to maintain rapamycin-resistant phosphorylation of the translational repressor 4E-BP1 and phosphorylation of the BH3 protein BAD [2].
The serine/threonine kinase Pim-2 is a transcriptionally regulated apoptotic inhibitor [2].
In monoclonal Ig-transgenic mice, each autoantigen binding B cell receives elevated amounts of BAFF, exhibiting increased levels of NFkappaB p52 and of the prosurvival kinase Pim2 [3].
Here we demonstrate that Pim-1, a serine/threonine kinase closely related to Pim-2 and Pim-3, is induced in hippocampus in response to stimuli that evoke long-term potentiation (LTP) [4].
However, they fail to consolidate enduring LTP even though Pim-2 and Pim-3 are constitutively expressed in the hippocampus and Pim-3 expression is similarly induced by synaptic activity [4].

Biological context of Pim2

Proviral tagging in E mu-myc transgenic mice lacking the Pim-1 proto-oncogene leads to compensatory activation of Pim-2 [5].
Pim-2 transgene induces lymphoid tumors, exhibiting potent synergy with c-myc [6].
Pim-2 is a transcriptionally regulated oncogenic kinase that promotes cell survival in response to a wide variety of proliferative signals [7].
The ability of Pim-2 to serve as an oncogene in vivo depends on sustained NF-kappaB activity [7].
Although Pim-2 cooperates with Myc to promote growth factor-independent cell proliferation, this feature is abrogated by NF-kappaB blockade [7].

Anatomical context of Pim2

Lymphocyte transformation by Pim-2 is dependent on nuclear factor-kappaB activation [7].

Other interactions of Pim2

Thus, the transcriptional induction of Pim-2 initiates a novel NF-kappaB activation pathway that regulates cell survival [7].
Structural features suggest that like the mouse Pim-2, hPim-2 is also a serine threonine kinase [8].

References

Pim kinases phosphorylate multiple sites on Bad and promote 14-3-3 binding and dissociation from Bcl-XL. Macdonald, A., Campbell, D.G., Toth, R., McLauchlan, H., Hastie, C.J., Arthur, J.S. BMC Cell Biol. (2006) [Pubmed]
The serine/threonine kinase Pim-2 is a transcriptionally regulated apoptotic inhibitor. Fox, C.J., Hammerman, P.S., Cinalli, R.M., Master, S.R., Chodosh, L.A., Thompson, C.B. Genes Dev. (2003) [Pubmed]
Reduced competitiveness of autoantigen-engaged B cells due to increased dependence on BAFF. Lesley, R., Xu, Y., Kalled, S.L., Hess, D.M., Schwab, S.R., Shu, H.B., Cyster, J.G. Immunity (2004) [Pubmed]
Pim kinase expression is induced by LTP stimulation and required for the consolidation of enduring LTP. Konietzko, U., Kauselmann, G., Scafidi, J., Staubli, U., Mikkers, H., Berns, A., Schweizer, M., Waltereit, R., Kuhl, D. EMBO J. (1999) [Pubmed]
Proviral tagging in E mu-myc transgenic mice lacking the Pim-1 proto-oncogene leads to compensatory activation of Pim-2. van der Lugt, N.M., Domen, J., Verhoeven, E., Linders, K., van der Gulden, H., Allen, J., Berns, A. EMBO J. (1995) [Pubmed]
Pim-2 transgene induces lymphoid tumors, exhibiting potent synergy with c-myc. Allen, J.D., Verhoeven, E., Domen, J., van der Valk, M., Berns, A. Oncogene (1997) [Pubmed]
Lymphocyte transformation by Pim-2 is dependent on nuclear factor-kappaB activation. Hammerman, P.S., Fox, C.J., Cinalli, R.M., Xu, A., Wagner, J.D., Lindsten, T., Thompson, C.B. Cancer Res. (2004) [Pubmed]
The human Pim-2 proto-oncogene and its testicular expression. Baytel, D., Shalom, S., Madgar, I., Weissenberg, R., Don, J. Biochim. Biophys. Acta (1998) [Pubmed]

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