Identification and analysis of a novel dimerization domain shared by various members of c-jun n-terminal kinase (jnk) scaffold proteins

Ksenya Cohen-Katsenelson, Tanya Wasserman, Ilona Darlyuk-Saadon, Alona Rabner, Fabian Glaser, Ami Aronheim

نتاج البحث: نشر في مجلةمقالةمراجعة النظراء

ملخص

Background: WDR62 is a JNK scaffold protein. Results: We identified at the WDR62 C terminus a loop-helix domain that is responsible for its homodimerization and association with another JNK scaffold protein, MAPKBP1. WDR62 dimerization is required for JNK and MKK7β1 recruitment. Conclusion: WDR62 dimerization is required for its scaffolding function. Significance: Scaffold protein association offers another layer of complexity for the fine tuning of signaling pathways.

اللغة الأصليةالإنجليزيّة
الصفحات (من إلى)7294-7304
عدد الصفحات11
دوريةJournal of Biological Chemistry
مستوى الصوت288
رقم الإصدار10
المعرِّفات الرقمية للأشياء
حالة النشرنُشِر - 8 مارس 2013

All Science Journal Classification (ASJC) codes

  • !!Biochemistry
  • !!Molecular Biology
  • !!Cell Biology

بصمة

أدرس بدقة موضوعات البحث “Identification and analysis of a novel dimerization domain shared by various members of c-jun n-terminal kinase (jnk) scaffold proteins'. فهما يشكلان معًا بصمة فريدة.

قم بذكر هذا