Prolin-rich tyrosine kinase 2 (PYK2) expression and localization in mouse testis

Paolo Chieffi, Marco Barchi, Silvia Di Agostino, Pellegrino Rossi, Donatella Tramontano, Raffaele Geremia

Research output: Contribution to journalArticlepeer-review


Prolin-rich kinase 2 (PYK2) is a nonreceptor tyrosine kinase related to the focal adhesion kinase (FAK) p125FAK. PYK2 is rapidly phosphorylated on tyrosine residues in response to various stimuli, such as tumor necrosis factor-α (TNF-α), changes in osmolarity, elevation in intracellular calcium concentration, angiotensin, and UV irradiation. PYK2 has ligand sequences for Src homology 2 and 3 (SH-2 and SH-3), and has binding sites for paxillin and p130cas. Activation of PYK2 leads to modulation of ion channel function, phosphorylation of tyrosine residues, and activation of the MAP kinase signaling pathways. Immunocytochemistry shows that PYK2 is present in mouse germinal and Sertoli cells (ser). 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.

Original languageEnglish
Pages (from-to)330-335
Number of pages6
JournalMolecular Reproduction and Development
Issue number3
Publication statusPublished - Jul 1 2003


  • Focal adhesion kinase
  • Phosphorylation
  • Spermatogenesis

ASJC Scopus subject areas

  • Cell Biology
  • Developmental Biology
  • Genetics


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