کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2041085 1073144 2015 13 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
A Cell-Signaling Network Temporally Resolves Specific versus Promiscuous Phosphorylation
ترجمه فارسی عنوان
یک شبکه سلولی-سیگنالینگ به طور موقت فسفریلاسیون خاصی در مقابل تشعشعات را حل می کند
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک علوم کشاورزی و بیولوژیک (عمومی)
چکیده انگلیسی


• A strategy for phosphoproteomics at high temporal resolution and coverage
• The HOG-signaling network involves 25% of the kinome and 10% of phosphatases
• Changes in functional phosphorylation occur more rapidly than promiscuous events
• Many potentially regulatory phosphosites in cytoskeletal proteins are reported

SummaryIf specific and functional kinase- or phosphatase-substrate interactions are optimized for binding compared to promiscuous interactions, then changes in phosphorylation should occur faster on functional versus promiscuous substrates. To test this hypothesis, we designed a high temporal resolution global phosphoproteomics protocol to study the high-osmolarity glycerol (HOG) response in the budding yeast Saccharomyces cerevisiae. The method provides accurate, stimulus-specific measurement of phosphoproteome changes, quantitative analysis of phosphodynamics at sub-minute temporal resolution, and detection of more phosphosites. Rates of evolution of dynamic phosphosites were comparable to those of known functional phosphosites and significantly lower than static or longer-time-frame dynamic phosphosites. Kinetic profile analyses indicated that putatively functional kinase- or phosphatase-substrate interactions occur more rapidly, within 60 s, than promiscuous interactions. Finally, we report many changes in phosphorylation of proteins implicated in cytoskeletal and mitotic spindle dynamics that may underlie regulation of cell cycle and morphogenesis.

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: - Volume 10, Issue 7, 24 February 2015, Pages 1202–1214
نویسندگان
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