کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5527337 | 1401578 | 2016 | 37 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Distinct hydrophobic “patches” in the N- and C-tails of beta-catenin contribute to nuclear transport
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کلمات کلیدی
MBPβ-catGFPAPCNPCARMadenomatous polyposis coli - آدنوماتوز پولیپوزیس کولی یا آدنوماتوس پولیپوزیس کولای beta-catenin - بتا کاتینینβ-catenin - بتا-کاتنینBis-ANS - بیس-ANSLive cell imaging - تصویربرداری سلول زندهNuclear transport - حمل و نقل هسته ایWnt signaling - سیگنال Wntfluorescence recovery after photobleaching - فلوئورسانس پس از فوتوبلاسیکNup - قدم زدنnuclear pore complex - مجتمع مخرب هسته ایNuclear pore - منافذ هسته ایNucleoporin - نولولپورینgreen fluorescent protein - پروتئین فلورسنت سبزmaltose-binding protein - پروتئین متصل به مالتوز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
تحقیقات سرطان
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
β-catenin is a key mediator of Wnt signaling and its deregulated nuclear accumulation can drive cancer progression. While the central armadillo (Arm) repeats of β-catenin stimulate nuclear entry, the N- and C-terminal “tail” sequences are thought to regulate turnover and transactivation. We show here that the N- and C-tails are also potent transport sequences. The unstructured tails of β-catenin, when individually fused to a GFP-reporter, could enter and exit the nucleus rapidly in live cells. Proximity ligation assays and pull-down assays identified a weak interaction between the tail sequences and the FG-repeats of nucleoporins, consistent with a possible direct translocation of β-catenin through the nuclear pore complex. Extensive alanine mutagenesis of the tail sequences revealed that nuclear translocation of β-catenin was dependent on specific uniformly distributed patches of hydrophobic residues, whereas the mutagenesis of acidic amino acids had no effect. Moreover, the mutation of hydrophobic patches within the N-tail and C-tail of full length β-catenin reduced nuclear transport rate and diminished its ability to activate transcription. We propose that the tail sequences can contribute to β-catenin transport and suggest a possible similar role for hydrophobic unstructured regions in other proteins.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Experimental Cell Research - Volume 348, Issue 2, 1 November 2016, Pages 132-145
Journal: Experimental Cell Research - Volume 348, Issue 2, 1 November 2016, Pages 132-145
نویسندگان
Manisha Sharma, Cara Jamieson, Christina Lui, Beric R. Henderson,