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Gene Review

Pkn1  -  protein kinase N1

Mus musculus

Synonyms: DBK, F730027O18Rik, PAK1, PRK1, Pkn, ...
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Disease relevance of Pkn1

  • Identification of two eukaryote-like serine/threonine kinases encoded by Chlamydia trachomatis serovar L2 and characterization of interacting partners of Pkn1 [1].
  • CT145 and CT301 (encoding Pkn1 and PknD, respectively) were expressed in Escherichia coli as GST fusion proteins [1].
  • Finally, we found that consistent with a role in breast tumor progression, Pak1 expression and its nuclear accumulation was increased progressively during the transition from ductal hyperplasia to ductal carcinoma in situ to adenocarcinoma in widely used multistep polyoma-middle T-antigen transgenic mice [2].
  • Emerging data suggest that p21-activated kinase 1 (Pak1), a downstream signaling molecule of the small GTPases, growth factors, and lipid signaling, is upregulated or hyperactivated in human breast cancer [2].
  • Our results showed that in a transgenic mouse model, overexpression of catalytically active Pak1 leads to the development of malignant mammary tumors and to a variety of other breast lesions, including focal solid nodules, ductal hyperplasia, and mini-intraductal neoplasm and adenoma [2].

High impact information on Pkn1


Biological context of Pkn1


Anatomical context of Pkn1

  • We show that PSMA inhibition, knockdown, or deficiency decreases endothelial cell invasion in vitro via integrin and PAK, thus abrogating angiogenesis [10].
  • During closure of a fibroblast monolayer wound, Pak1 is rapidly activated and localizes to the leading edge of motile cells, then gradually tapers off as the wound closes [5].
  • In contrast, cells expressing a kinase-dead form of Pak1 projected multiple lamellipodia emerging from different parts of the cell simultaneously [6].
  • We established clonal tetracycline-regulated NIH-3T3 cell lines that inducibly express either wild-type Pak1, a kinase-dead, or constitutively-active forms of this enzyme, and examined the morphology, F-actin organization, and motility of these cells [6].
  • Because cell motility requires polarized rearrangements of the actin/myosin cytoskeleton, we examined the role of Pak1 in regulating cell movement [6].

Associations of Pkn1 with chemical compounds


Other interactions of Pkn1

  • Taken together, our findings present a pathway for the selective hyperosmotic-induced Rac1-dependent PKN1 translocation and PDK1-dependent activation [7].
  • Protein kinase N 1 (PKN1), which in part resembles yeast protein kinase C, has been shown to be under the control of Rho GTPases and 3-phosphoinositide-dependent kinase 1 (PDK1) [7].

Analytical, diagnostic and therapeutic context of Pkn1

  • Co-immunoprecipitation experiments demonstrate an in vivo interaction of PAK1 with filamentous (F)-actin in stimulated cells [13].
  • Microinjection of a constitutively active PAK1 mutant into Rat-1 fibroblasts overexpressing the insulin receptor (HIRcB cells) induced the formation of F-actin- and PAK1-containing structures reminiscent of dorsal ruffles [13].


  1. Identification of two eukaryote-like serine/threonine kinases encoded by Chlamydia trachomatis serovar L2 and characterization of interacting partners of Pkn1. Verma, A., Maurelli, A.T. Infect. Immun. (2003) [Pubmed]
  2. PAK1 hyperactivation is sufficient for mammary gland tumor formation. Wang, R.A., Zhang, H., Balasenthil, S., Medina, D., Kumar, R. Oncogene (2006) [Pubmed]
  3. Regulation of anchorage-dependent signal transduction by protein kinase A and p21-activated kinase. Howe, A.K., Juliano, R.L. Nat. Cell Biol. (2000) [Pubmed]
  4. The integrin-binding protein Nischarin regulates cell migration by inhibiting PAK. Alahari, S.K., Reddig, P.J., Juliano, R.L. EMBO J. (2004) [Pubmed]
  5. Temporal and spatial distribution of activated Pak1 in fibroblasts. Sells, M.A., Pfaff, A., Chernoff, J. J. Cell Biol. (2000) [Pubmed]
  6. p21-activated kinase 1 (Pak1) regulates cell motility in mammalian fibroblasts. Sells, M.A., Boyd, J.T., Chernoff, J. J. Cell Biol. (1999) [Pubmed]
  7. Hyperosmotic-induced protein kinase N 1 activation in a vesicular compartment is dependent upon Rac1 and 3-phosphoinositide-dependent kinase 1. Torbett, N.E., Casamassima, A., Parker, P.J. J. Biol. Chem. (2003) [Pubmed]
  8. Genetic deletion of Rac1 GTPase reveals its critical role in actin stress fiber formation and focal adhesion complex assembly. Guo, F., Debidda, M., Yang, L., Williams, D.A., Zheng, Y. J. Biol. Chem. (2006) [Pubmed]
  9. Cell cycle-regulated phosphorylation of p21-activated kinase 1. Thiel, D.A., Reeder, M.K., Pfaff, A., Coleman, T.R., Sells, M.A., Chernoff, J. Curr. Biol. (2002) [Pubmed]
  10. Prostate-specific membrane antigen regulates angiogenesis by modulating integrin signal transduction. Conway, R.E., Petrovic, N., Li, Z., Heston, W., Wu, D., Shapiro, L.H. Mol. Cell. Biol. (2006) [Pubmed]
  11. Constitutive activation of endocytosis by mutation of myoA, the myosin I gene of Aspergillus nidulans. Yamashita, R.A., May, G.S. J. Biol. Chem. (1998) [Pubmed]
  12. p85 beta-PIX is required for cell motility through phosphorylations of focal adhesion kinase and p38 MAP kinase. Lee, J., Jung, I.D., Chang, W.K., Park, C.G., Cho, d.o. .Y., Shin, E.Y., Seo, D.W., Kim, Y.K., Lee, H.W., Han, J.W., Lee, H.Y. Exp. Cell Res. (2005) [Pubmed]
  13. Localization of p21-activated kinase 1 (PAK1) to pinocytic vesicles and cortical actin structures in stimulated cells. Dharmawardhane, S., Sanders, L.C., Martin, S.S., Daniels, R.H., Bokoch, G.M. J. Cell Biol. (1997) [Pubmed]
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