کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10817079 | 1058655 | 2005 | 14 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
The last five amino acid residues at the C-terminus of PRK1/PKN is essential for full lipid responsiveness
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کلمات کلیدی
RMSDnPKCNovel PKCcPKCPDK-1aPKCPKBPKCpKaPAGE3-phosphoinositide-dependent kinase-1 - 3-فسفوئوزیتید وابسته به کیناز-1Atypical PKC - PKC آتیپیکpolyacrylamide gel electrophoresis - الکتروفورز ژل پلی آکریل آمیدroot mean square deviation - میانگین انحراف مربع ریشهwild-type - نوع وحشیprotein 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
PRK1/PKN is a member of the protein kinase C (PKC) superfamily of serine/threonine protein kinases. Despite its important role as a RhoA effector, limited information is available regarding how this kinase is regulated. We show here that the last seven amino acid residues at the C-terminus is dispensable for the catalytic activity of PRK1 but is critical for the in vivo stability of this kinase. Surprisingly, the intact hydrophobic motif in PRK1 is dispensable for 3-phosphoinositide-dependent kinase-1 (PDK-1) binding and phosphorylation of the activation loop, as the PRK1-Î940 mutant lacking the last two residues of the hydrophobic motif and the last 5 residues at the C-terminus interacts with PDK-1 in vivo and has a similar specific activity as the wild-type protein. We also found that the last four amino acid residues at the C-terminus of PRK1 is critical for the full lipid responsiveness as the PRK1-Î942 deletion mutant is no longer activated by arachidonic acid. Our data suggest that the very C-terminus in PRK1 is critically involved in the control of the catalytic activity and activation by lipids. Since this very C-terminal segment is the least conserved among members of the PKC superfamily, it would be a promising target for isozyme-specific pharmaceutical interventions.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Cellular Signalling - Volume 17, Issue 9, September 2005, Pages 1084-1097
Journal: Cellular Signalling - Volume 17, Issue 9, September 2005, Pages 1084-1097
نویسندگان
Wee Guan Lim, Yimin Zhu, Chern-Hoe Wang, Bee Jen Tan, Jeffrey S. Armstrong, Terje Dokland, Hongyuan Yang, Yi-Zhun Zhu, Tian Seng Teo, Wei Duan,