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STK16  -  serine/threonine kinase 16

Homo sapiens

Synonyms: KRCT, MPSK, MPSK1, Myristoylated and palmitoylated serine/threonine-protein kinase, PKL12, ...
 
 
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Disease relevance of STK16

  • To confirm these data in vivo, we injected tumor cells overexpressing STK16 into immunodeficient BALBc/SCID mice [1].
 

High impact information on STK16

  • PKL12 (STK16) is a ubiquitously expressed Ser/Thr kinase, not structurally related to the well known subfamilies, with a putative role in cell adhesion control [2].
  • These results are interpreted to indicate a potential in vivo role for GlcNAcK in PKL12 translocation and a tentative regulatory role for PKL12-mediated phosphorylation on substrate proteins [2].
  • After overexpression, GlcNAcK localizes in vesicular structures associated mainly with the cell membrane and colocalizes with the PKL12 protein [2].
  • In addition, we show that STK16 overexpression in several cell lines enhances their capacity to produce and secrete VEGF [1].
  • HT1080-derived tumors overexpressing STK16 showed increased volume and number of blood vessels compared to controls [1].
 

Biological context of STK16

  • Radiation hybridization localized the human MPSK gene to chromosome 2q34-37 [3].
 

Associations of STK16 with chemical compounds

  • Endogenous STK16 subcellular localization was evaluated by indirect immunofluorescence in NIH/3T3 and NRK cells, demonstrating a Golgi-associated pattern that appears to be independent of signals provided by integrin pathways [1].
  • The protein kinase has been accordingly denoted as the myristylated and palmitylated serine/threonine protein kinase (MPSK) [3].
  • Epitope tagged human MPSK was found to be acylated by myristic acid at glycine residue 2 and by palmitic acid at cysteines 6 and/or 8 [3].
  • While epitope tagged MPSK in immune complexes or purified human glutathione S transferase-MPSK was found to autophosphorylate at one or more threonine residues, the enzyme was not found to phosphorylate several other common exogenous substrates [3].
  • The small Photosystem I particles prepared from spinach chloroplasts by the action of Triton X-100 (TSF 1 particles) reaggregate into membrane structures when they are incubated with soybean phospholipids and cholate and then subjected to a slow dialysis [4].
 

Analytical, diagnostic and therapeutic context of STK16

  • RT-PCR analysis of several cell lines also supports this view, therefore suggesting that PKL12 may play a role in a very general cellular function, probably related with the secretory pathway [5].

References

  1. Nucleocytoplasmic shuttling of STK16 (PKL12), a Golgi-resident serine/threonine kinase involved in VEGF expression regulation. Guinea, B., Ligos, J.M., Laín de Lera, T., Martín-Caballero, J., Flores, J., Gonzalez de la Peña, M., García-Castro, J., Bernad, A. Exp. Cell Res. (2006) [Pubmed]
  2. Functional interaction between the Ser/Thr kinase PKL12 and N-acetylglucosamine kinase, a prominent enzyme implicated in the salvage pathway for GlcNAc recycling. Ligos, J.M., de Lera, T.L., Hinderlich, S., Guinea, B., Sánchez, L., Roca, R., Valencia, A., Bernad, A. J. Biol. Chem. (2002) [Pubmed]
  3. Identification and characterization of a myristylated and palmitylated serine/threonine protein kinase. Berson, A.E., Young, C., Morrison, S.L., Fujii, G.H., Sheung, J., Wu, B., Bolen, J.B., Burkhardt, A.L. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  4. Photophosphorylation and related properties of reaggregated vesicles from spinach photosystem I particles. Jaynes, J.M., Vernon, L.P., Klein, S.M. Biochim. Biophys. Acta (1975) [Pubmed]
  5. Cloning, expression analysis, and functional characterization of PKL12, a member of a new subfamily of ser/thr kinases. Ligos, J.M., Gerwin, N., Fernández, P., Gutierrez-Ramos, J.C., Bernad, A. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
 
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