کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9745100 | 1645297 | 2005 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Quantifying ERK2-protein interactions by fluorescence anisotropy: PEA-15 inhibits ERK2 by blocking the binding of DEJL domains
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کلمات کلیدی
EGFERK2YFPDEFFADDPEA-15FAS-associating protein with death domainCFPHEPESERK1/2 - ERK1 / 2PMA - LDC هاMAPK - MAPKMAPK kinase - MAPK کینازN-(2-Hydroxyethyl)piperazine-N′-2-ethanesulfonic acid - N- (2-Hydroxyethyl) piperazine-N'-2-ethanesulfonic acidFluorescence resonance energy transfer - انتقال انرژی رزونانس FluorescenceFRET - انتقال انرژی رزونانسی فورسترFluorescence anisotropy - بی خوابی فلورسانسیepidermal growth factor - عامل رشد اپیدرمیphorbol myristate acetate - فروبل مریستات استاتyellow fluorescent protein - پروتئین فلورسنت زردcyan fluorescent protein - پروتئین فلورسنت سیانوژنextracellular signal-regulated protein kinases 1 and 2 - پروتئین کیناز 1 و 2 تنظیم شده توسط سیگنال خارج سلولیmitogen-activated protein kinase - پروتئین کیناز فعال با mitogen
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
While mitogen-activated protein kinase signaling pathways constitute highly regulated networks of protein-protein interactions, little quantitative information for these interactions is available. Here we highlight recent fluorescence anisotropy binding studies that focus on the interactions of ERK1 and ERK2 with PEA-15 (antiapoptotic phosphoprotein enriched in astrocytes-15 kDa), a small protein that sequesters ERK2 in the cytoplasm. The regulation of ERK2 by PEA-15 is appraised in the light of a simple equilibrium-binding model for reversible ERK2 nucleoplasmic-cytoplasmic shuttling, which elaborates on the theory of Burack and Shaw (J. Biol. Chem. 280, 3832-3837; 2005). Also highlighted is the recent observation that the peptide N-QKGKPRDLELPLSPSL-C, derived from the docking site for ERK/JNK and LEL (DEJL) in Elk-1, displaces PEA-15 from ERK2. It is proposed that the C-terminus of PEA-15 (121LXLXXXXKK129) is a reverse DEJL domain [which has a general consensus of R/K-ÏA-X3/4-ÏB, where ÏA and ÏB are hydrophobic residues (Leu, Ile, or Val)], which mediates one arm of a bidentate PEA-15 interaction with ERK2. The notion that PEA-15 is a potent inhibitor of many ERK2-mediated phosphorylations, by virtue of its ability to block ERK2-DEJL domain interactions, is proposed.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1754, Issues 1â2, 30 December 2005, Pages 316-323
Journal: Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics - Volume 1754, Issues 1â2, 30 December 2005, Pages 316-323
نویسندگان
Kari Callaway, Mark A. Rainey, Kevin N. Dalby,