کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1964524 | 1058556 | 2006 | 12 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The very C-terminus of protein kinase CÉ is critical for the full catalytic competence but its hydrophobic motif is dispensable for the interaction with 3-phosphoinositide-dependent kinase-1
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کلمات کلیدی
PKCnPKCNovel PKCcPKCPDK-1aPKCPKCɛPKBpKaPAGE12-O-tetradecanoylphorbol-13-acetatetPARMSD3-phosphoinositide-dependent kinase-1 - 3-فسفوئوزیتید وابسته به کیناز-1Atypical PKC - PKC آتیپیکpolyacrylamide gel electrophoresis - الکتروفورز ژل پلی آکریل آمیدMolecular dynamics - دینامیک ملکولی یا پویایی مولکولیPhosphorylation - فسفریلاسیونHydrophobic motif - موتیف هیدروفوبroot mean square deviation - میانگین انحراف مربع ریشهwild-type - نوع وحشیSignal transduction - هدایت سیگنالprotein kinase B - پروتئین کیناز BProtein kinase C - پروتئین کیناز سیcAMP-dependent protein kinase - پروتئین کیناز وابسته به cAMP
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
In this article, we explore the role of the C-terminus (V5 domain) of PKCÉ plays in the catalytic competence of the kinase using serial truncations followed by immune-complex kinase assays. Surprisingly, removal of the last seven amino acid residues at the C-terminus of PKCÉ resulted in a PKCÉ-Î731 mutant with greatly reduced intrinsic catalytic activity while truncation of eight amino acid residues at the C-terminus resulted in a catalytically inactive PKCÉ mutant. Computer modeling and molecular dynamics simulations showed that the last seven and/or eight amino acid residues of PKCÉ were involved in interactions with residues in the catalytic core. Further truncation analyses revealed that the hydrophobic phosphorylation motif was dispensable for the physical interaction between PKCÉ and 3-phosphoinositide-dependent kinase-1 (PDK-1) as the PKCÉ mutant lacking both the turn and the hydrophobic motifs could still be co-immunoprecipitated with PDK-1. These results provide fresh insights into the biochemical and structural basis underlying the isozyme-specific regulation of PKC and suggest that the very C-termini of PKCs constitute a promising new target for the development of novel isozyme-specific inhibitors of PKC.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Cellular Signalling - Volume 18, Issue 6, June 2006, Pages 807-818
Journal: Cellular Signalling - Volume 18, Issue 6, June 2006, Pages 807-818
نویسندگان
Yimin Zhu, Derek Smith, Chandra Verma, Wee Guan Lim, Bee Jen Tan, Jeffrey S. Armstrong, Shufeng Zhou, Eli Chan, Seng-Lai Tan, Yi-Zhun Zhu, Nam Sang Cheung, Wei Duan,