دورية أكاديمية
أعرض في EDS

KRAS Protein Stability Is Regulated through SMURF2: UBCH5 Complex-Mediated β-TrCP1 Degradation

التفاصيل البيبلوغرافية
العنوان: KRAS Protein Stability Is Regulated through SMURF2: UBCH5 Complex-Mediated β-TrCP1 Degradation
المؤلفون: Shirish Shukla, Uday Sankar Allam, Aarif Ahsan, Guoan Chen, Pranathi Meda Krishnamurthy, Katherine Marsh, Matthew Rumschlag, Sunita Shankar, Christopher Whitehead, Matthew Schipper, Venkatesha Basrur, Daniel R. Southworth, Arul M. Chinnaiyan, Alnawaz Rehemtulla, David G. Beer, Theodore S. Lawrence, Mukesh K. Nyati, Dipankar Ray
المصدر: Neoplasia: An International Journal for Oncology Research, Vol 16, Iss 2, Pp 115-128 (2014)
بيانات النشر: Elsevier, 2014.
سنة النشر: 2014
المجموعة: LCC:Neoplasms. Tumors. Oncology. Including cancer and carcinogens
مصطلحات موضوعية: Neoplasms. Tumors. Oncology. Including cancer and carcinogens, RC254-282
الوصف: Attempts to target mutant KRAS have been unsuccessful. Here, we report the identification of Smad ubiquitination regulatory factor 2 (SMURF2) and UBCH5 as a critical E3:E2 complex maintaining KRAS protein stability. Loss of SMURF2 either by small interfering RNA/short hairpin RNA (siRNA/shRNA) or by overexpression of a catalytically inactive mutant causes KRAS degradation, whereas overexpression of wild-type SMURF2 enhances KRAS stability. Importantly, mutant KRAS is more susceptible to SMURF2 loss where protein half-life decreases from >12 hours in control siRNA-treated cells to
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1476-5586
1522-8002
Relation: http://www.sciencedirect.com/science/article/pii/S1476558614800110; https://doaj.org/toc/1476-5586; https://doaj.org/toc/1522-8002
DOI: 10.1593/neo.14184
URL الوصول: https://doaj.org/article/337e778e43f7471c962968f288517f18
رقم الأكسشن: edsdoj.337e778e43f7471c962968f288517f18
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:14765586
15228002
DOI:10.1593/neo.14184