کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10759550 | 1050425 | 2013 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Ubiquitination and degradation of the hominoid-specific oncoprotein TBC1D3 is regulated by protein palmitoylation
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کلمات کلیدی
EGFRCUL7Protein ubiquitinationIRS-1FCSIGF-1PP2AGAPDHPBSEGFGTPase Activating Protein - GTPase فعال کردن پروتئینOncogene - انکوژنProtein degradation - تخریب پروتئینCancer - سرطانfetal calf serum - سرم گوساله جنینGAP - شکافepidermal growth factor - عامل رشد اپیدرمیPhosphate-buffered saline - محلول نمک فسفات با خاصیت بافریProtein palmitoylation - پروتئین palmitoylationprotein phosphatase 2A - پروتئین فسفاتاز 2Aglyceraldehyde-3-phosphate dehydrogenase - گلیسرالیدید-3-فسفات دهیدروژنازinsulin receptor - گیرنده انسولینEpidermal growth factor receptor - گیرنده فاکتور رشد اپیدرمال
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Ubiquitination and degradation of the hominoid-specific oncoprotein TBC1D3 is regulated by protein palmitoylation Ubiquitination and degradation of the hominoid-specific oncoprotein TBC1D3 is regulated by protein palmitoylation](/preview/png/10759550.png)
چکیده انگلیسی
Expression of the hominoid-specific oncoprotein TBC1D3 promotes enhanced cell growth and proliferation by increased activation of signal transduction through several growth factors. Recently we documented the role of CUL7 E3 ligase in growth factors-induced ubiquitination and degradation of TBC1D3. Here we expanded our study to discover additional molecular mechanisms that control TBC1D3 protein turnover. We report that TBC1D3 is palmitoylated on two cysteine residues: 318 and 325. The expression of double palmitoylation mutant TBC1D3:C318/325S resulted in protein mislocalization and enhanced growth factors-induced TBC1D3 degradation. Moreover, ubiquitination of TBC1D3 via CUL7 E3 ligase complex was increased by mutating the palmitoylation sites, suggesting that depalmitoylation of TBC1D3 makes the protein more available for ubiquitination and degradation. The results reported here provide novel insights into the molecular mechanisms that govern TBC1D3 protein degradation. Dysregulation of these mechanisms in vivo could potentially result in aberrant TBC1D3 expression and promote oncogenesis.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 434, Issue 2, 3 May 2013, Pages 388-393
Journal: Biochemical and Biophysical Research Communications - Volume 434, Issue 2, 3 May 2013, Pages 388-393
نویسندگان
Chen Kong, Jeffrey J. Lange, Dmitri Samovski, Xiong Su, Jialiu Liu, Sinju Sundaresan, Philip D. Stahl,