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c‐Raf kinase binds to N‐terminal domain of c‐Myc
Author(s) -
Ivan Alexandrov,
Larisa Shlyakhova,
A. A. Vartanyan,
Maria Zajac-Kaye,
N. Alexandrova
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00992-7
Subject(s) - kinase , in vitro , chemistry , terminal (telecommunication) , amino terminal , protein kinase a , protein kinase domain , phosphorylation , biochemistry , cyclin dependent kinase 9 , microbiology and biotechnology , mitogen activated protein kinase kinase , biology , peptide sequence , gene , computer science , mutant , telecommunications
We have demonstrated that the 50 N‐terminal amino acids of c‐Myc bind a kinase activity, which phosphorylates Myc in vitro predominantly on Thr 8 . We also have shown that c‐Raf, a widely known Ser/Thr kinase, involved in the Ras signaling pathway, binds to the same portion of c‐Myc in vitro. In addition we were able to precipitate native c‐Myc/Raf complex from various cell lysates. Physical interaction of Myc and Raf may potentially be a part of their well‐known functional cooperation.