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|Title:||Expression of receptor-like protein tyrosine phosphatase a in rat embryo fibroblasts activates mitogen-activated protein kinase and c-Jun||Authors:||Zheng, X.M.
|Issue Date:||16-Sep-1994||Citation:||Zheng, X.M.,Pallen, C.J. (1994-09-16). Expression of receptor-like protein tyrosine phosphatase a in rat embryo fibroblasts activates mitogen-activated protein kinase and c-Jun. Journal of Biological Chemistry 269 (37) : 23302-23309. ScholarBank@NUS Repository.||Abstract:||Anti-c-Src and anti-phosphotyrosine immunoprecipitates from receptor-like protein tyrosine phosphatase a (PTPα)-transfected and control rat embryo fibroblasts contain a 39-kDa phosphoprotein (p39) whose phosphorylation is enhanced by PTPα expression. The p39 that co-immunoprecipitates with c-Src has been identified as c-Jun by immunological and functional criteria; it is recognized by several different anti-c-Jun antibodies and binds to a c-Jun recognition element-containing oligonucleotide. Whereas the association of c-Src and c-Jun is unexpected, it may be of significance in PTPα signaling since we have previously demonstrated that c-Src is activated by PTPα (Zheng, X. M., Wang, Y., and Pallen, C. J. (1992) Nature 359, 336-339. Examination of c-Jun activity in these fibroblasts demonstrates that c-Jun DNA binding activity and c-Jun-mediated transcription of a chloramphenicol acetyltransferase reporter gene are elevated in PTPα-expressing cells. In addition to c-Jun activation, mitogen-activated protein kinase is activated in α-expressing cells and translocated to the nuclei of these cells. The nuclear localization of activated mitogen-activated protein kinase and c-Jun suggests that their activation represents downstream events in the receptor-like PTPα-initiated signaling pathway(s).||Source Title:||Journal of Biological Chemistry||URI:||http://scholarbank.nus.edu.sg/handle/10635/111882||ISSN:||00219258|
|Appears in Collections:||Staff Publications|
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