کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
8340617 1541247 2015 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Kinases, tails and more: Regulation of PTEN function by phosphorylation
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Kinases, tails and more: Regulation of PTEN function by phosphorylation
چکیده انگلیسی
Phosphorylation regulates the conformation, stability, homo- and heterotypic protein interactions, localization, and activity of the tumor suppressor PTEN. From a simple picture, at the beginning of this millennium, recognizing that CK2 phosphorylated PTEN at the C-terminus and thereby impacted on PTEN stability and activity, research has led to a significantly more complex scenario today, where for instance GSK3, Plk3, ATM, ROCK or Src-family kinases are also gaining the spotlight in this evolving play. Here, we review the current knowledge on the kinases that phosphorylate PTEN, and on the impact that specific phosphorylation events have on PTEN function.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Methods - Volumes 77–78, 1 May 2015, Pages 75-81
نویسندگان
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