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Prolin‐rich tyrosine kinase 2 (PYK2) expression and localization in mouse testis
Author(s) -
Chieffi Paolo,
Barchi Marco,
Di Agostino Silvia,
Rossi Pellegrino,
Tramontano Donatella,
Geremia Raffaele
Publication year - 2003
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/mrd.10297
Subject(s) - ptk2 , biology , proto oncogene tyrosine protein kinase src , tyrosine kinase , microbiology and biotechnology , tyrosine phosphorylation , tyrosine , phosphorylation , receptor tyrosine kinase , ror1 , signal transduction , mitogen activated protein kinase kinase , biochemistry , platelet derived growth factor receptor , protein kinase a , receptor , growth factor
Prolin‐rich kinase 2 (PYK2) is a nonreceptor tyrosine kinase related to the focal adhesion kinase (FAK) p125 FAK . 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 p130 cas . 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. Mol. Reprod. Dev. 65: 330–335, 2003. © 2003 Wiley‐Liss, Inc.