The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Ptk2b  -  PTK2 protein tyrosine kinase 2 beta

Mus musculus

Synonyms: CADTK, CAK-beta, CAKB, CAKbeta, Calcium-dependent tyrosine kinase, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Ptk2b


High impact information on Ptk2b

  • Here we demonstrate that a deficiency of the tyrosine kinase (Pyk-2) results in a cell autonomous defect of MZB cell production [7].
  • Absence of marginal zone B cells in Pyk-2-deficient mice defines their role in the humoral response [7].
  • In response to repetitive polysaccharide antigens (T-independent type II (TI-II)) Pyk-2-deficient mice displayed marked suppression of IgM, IgG3 and IgG2a production [7].
  • This information delimits the set of SH2-containing effectors available for PTK signaling and will facilitate the systems-level analysis of pTyr-dependent protein-protein interactions and PTK-mediated signal transduction [8].
  • Moreover, Akt/PKB can phosphorylate tuberin in vitro and in vivo [9].

Chemical compound and disease context of Ptk2b


Biological context of Ptk2b


Anatomical context of Ptk2b


Associations of Ptk2b with chemical compounds


Physical interactions of Ptk2b

  • Eliminating the Src-binding site on Pyk2 (Pyk2(Y402F)) markedly inhibited bone resorption by osteoclast-like cells, whereas kinase-dead Pyk2 had little effect [21].

Enzymatic interactions of Ptk2b


Regulatory relationships of Ptk2b


Other interactions of Ptk2b


Analytical, diagnostic and therapeutic context of Ptk2b

  • By Northern blot analysis, RAFTK is expressed in myeloid, lymphoid, and megakaryocytic hematopoietic cells [15].
  • Northern blot and immunoprecipitation analysis demonstrate that, among germinal cells, PYK2 is more abundant in spermatocytes (spc) and spermatids (spt); in addition, immunofluorescence analysis clearly shows that the diffuse cytoplasmic localization of PYK2 changes in a specific cellular compartment in spt and spermatozoa [17].
  • Confocal microscopy with use of fluorescent anti-Ti mAb revealed that the inhibition of TCR internalization corresponded to the induction of large patches that were localized in cell membrane areas depleted of polymerized actin, the formation of which was dependent on the combined action of the anti-Ti mAb and the PTK inhibitors [30].
  • In situ hybridization studies of rat brain demonstrate that the unspliced PYK2 is selectively expressed at high levels in hippocampus, cerebral cortex and olfactory bulb, whereas PYK2s and PRNK are expressed at low levels in all regions of rat brain examined [31].
  • As protein tyrosine phosphorylation is a requisite event induced by a majority of surface receptors, and protein tyrosine kinases of the src-family (src-PTKs) act as proximal transducers for many hematopoietic receptors, we have designed a quantitative RT-PCR assay to measure src-family PTK expression during critical stages of lymphocyte ontogeny [32].


  1. PYK2 in osteoclasts is an adhesion kinase, localized in the sealing zone, activated by ligation of alpha(v)beta3 integrin, and phosphorylated by src kinase. Duong, L.T., Lakkakorpi, P.T., Nakamura, I., Machwate, M., Nagy, R.M., Rodan, G.A. J. Clin. Invest. (1998) [Pubmed]
  2. Oncoprotein Akt/PKB induces trophic effects in murine models of Parkinson's disease. Ries, V., Henchcliffe, C., Kareva, T., Rzhetskaya, M., Bland, R., During, M.J., Kholodilov, N., Burke, R.E. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  3. Inhibition of osteoclast function by adenovirus expressing antisense protein-tyrosine kinase 2. Duong, L.T., Nakamura, I., Lakkakorpi, P.T., Lipfert, L., Bett, A.J., Rodan, G.A. J. Biol. Chem. (2001) [Pubmed]
  4. Defective proximal TCR signaling inhibits CD8+ tumor-infiltrating lymphocyte lytic function. Koneru, M., Schaer, D., Monu, N., Ayala, A., Frey, A.B. J. Immunol. (2005) [Pubmed]
  5. Cas, Fak and Pyk2 function in diverse signaling cascades to promote Yersinia uptake. Bruce-Staskal, P.J., Weidow, C.L., Gibson, J.J., Bouton, A.H. J. Cell. Sci. (2002) [Pubmed]
  6. Defective microtubule-dependent podosome organization in osteoclasts leads to increased bone density in Pyk2(-/-) mice. Gil-Henn, H., Destaing, O., Sims, N.A., Aoki, K., Alles, N., Neff, L., Sanjay, A., Bruzzaniti, A., De Camilli, P., Baron, R., Schlessinger, J. J. Cell Biol. (2007) [Pubmed]
  7. Absence of marginal zone B cells in Pyk-2-deficient mice defines their role in the humoral response. Guinamard, R., Okigaki, M., Schlessinger, J., Ravetch, J.V. Nat. Immunol. (2000) [Pubmed]
  8. The human and mouse complement of SH2 domain proteins-establishing the boundaries of phosphotyrosine signaling. Liu, B.A., Jablonowski, K., Raina, M., Arcé, M., Pawson, T., Nash, P.D. Mol. Cell (2006) [Pubmed]
  9. Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway. Manning, B.D., Tee, A.R., Logsdon, M.N., Blenis, J., Cantley, L.C. Mol. Cell (2002) [Pubmed]
  10. Role of PYK2 in the development of obesity and insulin resistance. Yu, Y., Ross, S.A., Halseth, A.E., Hollenbach, P.W., Hill, R.J., Gulve, E.A., Bond, B.R. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  11. Induction of apoptosis after expression of PYK2, a tyrosine kinase structurally related to focal adhesion kinase. Xiong, W., Parsons, J.T. J. Cell Biol. (1997) [Pubmed]
  12. Inhibition of PYK2-induced actin cytoskeleton reorganization, PYK2 autophosphorylation and focal adhesion targeting by FAK. Du, Q.S., Ren, X.R., Xie, Y., Wang, Q., Mei, L., Xiong, W.C. J. Cell. Sci. (2001) [Pubmed]
  13. Integrin-mediated signal transduction in cells lacking focal adhesion kinase p125FAK. Ueki, K., Mimura, T., Nakamoto, T., Sasaki, T., Aizawa, S., Hirai, H., Yano, S., Naruse, T., Nojima, Y. FEBS Lett. (1998) [Pubmed]
  14. PYK2 is an adhesion kinase in macrophages, localized in podosomes and activated by beta(2)-integrin ligation. Duong, L.T., Rodan, G.A. Cell Motil. Cytoskeleton (2000) [Pubmed]
  15. The related adhesion focal tyrosine kinase forms a complex with paxillin in hematopoietic cells. Salgia, R., Avraham, S., Pisick, E., Li, J.L., Raja, S., Greenfield, E.A., Sattler, M., Avraham, H., Griffin, J.D. J. Biol. Chem. (1996) [Pubmed]
  16. Mechanical strain on osteoblasts activates autophosphorylation of focal adhesion kinase and proline-rich tyrosine kinase 2 tyrosine sites involved in ERK activation. Boutahar, N., Guignandon, A., Vico, L., Lafage-Proust, M.H. J. Biol. Chem. (2004) [Pubmed]
  17. Prolin-rich tyrosine kinase 2 (PYK2) expression and localization in mouse testis. Chieffi, P., Barchi, M., Di Agostino, S., Rossi, P., Tramontano, D., Geremia, R. Mol. Reprod. Dev. (2003) [Pubmed]
  18. Mitogen-Activated Protein Kinases Inhibit the ROMK (Kir 1.1)-Like Small Conductance K Channels in the Cortical Collecting Duct. Babilonia, E., Li, D., Wang, Z., Sun, P., Lin, D.H., Jin, Y., Wang, W.H. J. Am. Soc. Nephrol. (2006) [Pubmed]
  19. Calcineurin is essential for depolarization-induced nuclear translocation and tyrosine phosphorylation of PYK2 in neurons. Faure, C., Corvol, J.C., Toutant, M., Valjent, E., Hvalby, O., Jensen, V., El Messari, S., Corsi, J.M., Kadaré, G., Girault, J.A. J. Cell. Sci. (2007) [Pubmed]
  20. Analysis of the calcium-dependent regulation of proline-rich tyrosine kinase 2 by gonadotropin-releasing hormone. Xie, J., Allen, K.H., Marguet, A., Berghorn, K.A., Bliss, S.P., Navratil, A.M., Guan, J.L., Roberson, M.S. Mol. Endocrinol. (2008) [Pubmed]
  21. Src kinase activity is essential for osteoclast function. Miyazaki, T., Sanjay, A., Neff, L., Tanaka, S., Horne, W.C., Baron, R. J. Biol. Chem. (2004) [Pubmed]
  22. Different modes and qualities of tyrosine phosphorylation of Fak and Pyk2 during epithelial-mesenchymal transdifferentiation and cell migration: analysis of specific phosphorylation events using site-directed antibodies. Nakamura, K., Yano, H., Schaefer, E., Sabe, H. Oncogene (2001) [Pubmed]
  23. Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2. Owen, J.D., Ruest, P.J., Fry, D.W., Hanks, S.K. Mol. Cell. Biol. (1999) [Pubmed]
  24. Cooperative inhibition of T-cell antigen receptor signaling by a complex between a kinase and a phosphatase. Cloutier, J.F., Veillette, A. J. Exp. Med. (1999) [Pubmed]
  25. Osmotic shock stimulates GLUT4 translocation in 3T3L1 adipocytes by a novel tyrosine kinase pathway. Chen, D., Elmendorf, J.S., Olson, A.L., Li, X., Earp, H.S., Pessin, J.E. J. Biol. Chem. (1997) [Pubmed]
  26. Inhibition of SRC tyrosine kinases suppresses activation of nuclear factor-kappaB, and serine and tyrosine phosphorylation of IkappaB-alpha in lipopolysaccharide-stimulated raw 264.7 macrophages. Kang, J.L., Lee, H.W., Kim, H.J., Lee, H.S., Castranova, V., Lim, C.M., Koh, Y. J. Toxicol. Environ. Health Part A (2005) [Pubmed]
  27. Stable association of PYK2 and p130(Cas) in osteoclasts and their co-localization in the sealing zone. Lakkakorpi, P.T., Nakamura, I., Nagy, R.M., Parsons, J.T., Rodan, G.A., Duong, L.T. J. Biol. Chem. (1999) [Pubmed]
  28. In vivo and in vitro specificity of protein tyrosine kinases for immunoglobulin G receptor (FcgammaRII) phosphorylation. Bewarder, N., Weinrich, V., Budde, P., Hartmann, D., Flaswinkel, H., Reth, M., Frey, J. Mol. Cell. Biol. (1996) [Pubmed]
  29. Developmental abnormalities of myelin basic protein expression in fyn knock-out brain reveal a role of Fyn in posttranscriptional regulation. Lu, Z., Ku, L., Chen, Y., Feng, Y. J. Biol. Chem. (2005) [Pubmed]
  30. Evidence for protein tyrosine kinase involvement in ligand-induced TCR/CD3 internalization and surface redistribution. Luton, F., Buferne, M., Davoust, J., Schmitt-Verhulst, A.M., Boyer, C. J. Immunol. (1994) [Pubmed]
  31. Expression and characterization of splice variants of PYK2, a focal adhesion kinase-related protein. Xiong, W.C., Macklem, M., Parsons, J.T. J. Cell. Sci. (1998) [Pubmed]
  32. Regulation of Src-family protein tyrosine kinase transcription during lymphocyte ontogeny. Longo, N.S., Wang, X., Wildin, R.S., Abraham, K.M. Mol. Immunol. (1999) [Pubmed]
WikiGenes - Universities