A PKC‐mediated backup mechanism of the MXXCW motif‐linked switch for initiating tyrosine kinase activities | Zendy

Takeda Kozue | Zendy; Kawamoto Yoshiyuki | Zendy; Okuno Yusuke | Zendy; Kato Masashi | Zendy; Takahashi Masahide | Zendy; Suzuki Haruhiko | Zendy; Isobe Kenichi | Zendy; Nakashima Izumi | Zendy

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A PKC‐mediated backup mechanism of the MXXCW motif‐linked switch for initiating tyrosine kinase activities

Author(s) -

Takeda Kozue,

Kawamoto Yoshiyuki,

Okuno Yusuke,

Kato Masashi,

Takahashi Masahide,

Suzuki Haruhiko,

Isobe Kenichi,

Nakashima Izumi

Publication year - 2006

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/j.febslet.2006.01.005

Subject(s) - threonine , serine , tyrosine , phosphorylation , protein kinase c , tyrosine kinase , mutant , cysteine , biochemistry , kinase , tyrosine phosphorylation , chemistry , microbiology and biotechnology , biology , signal transduction , enzyme , gene

The cysteine in the M/IXXCW motif is conserved in all but one (threonine in place of cysteine) of the human protein tyrosine kinases (PTKs). We showed that all RET‐PTC‐1 mutants in which the C in this motif (C376) was replaced with glycine, lysine, threonine or serine lost their activity in vitro. However, the C376T/S mutants showed normal tyrosine phosphorylation in vivo (in cells). Further analyses reveled that protein kinase C (PKC) initiated the activities of the C376T/S mutants in cells. We conclude that the M/IXXCW motif‐mediated mechanisms which initiate PTK activities are partially replaced by a PKC‐mediated mechanism.

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