AKT-dependent phosphorylation of the SAM domain induces oligomerization and activation of the scaffold protein CNK1

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• 作者：Adrian Fischer^a ; ^b ; ^c ; ^{adrian.fischer@biologie.uni-freiburg.de} ; Wilfried Weber^a ; ^b ; ^{wilfried.weber@biologie.uni-freiburg.de} ; Bettina Warscheid^b ; ^c ; ^{bettina.warscheid@biologie.uni-freiburg.de} ; Gerald Radziwill^a ; ^b ; ^c ; ^{gerald.radziwill@bioss.uni-freiburg.de}
• 关键词：ARF ; ADP ribosylation factor ; CNK ; connector enhancer of KSR ; ERK ; extracellular signal-regulated protein kinase ; EGF ; epidermal growth factor ; GF ; growth factor ; IGF ; insulin-like growth factor ; MAPK ; mitogen-activated protein kinase ; MEK ; MAPK/ERK kinase ; MMP ; matrix metalloproteinase ; PDGF ; platelet-derived growth factor ; PI3K ; phosphoinositide 3-kinase ; SAM ; sterile alpha motif
• 刊名：Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：1864
• 期：1
• 页码：89-100
• 全文大小：2994 K
• 卷排序：1864

文摘

AKT-dependent phosphorylation of Ser22 located within the SAM domain induces oligomerization. Oligomeric CNK1 increases affinity to AKT. Oligomerization of CNK1 activates CNK1-mediated signaling. A phosphomimetic mutant at Thr8 counteracts stimulation of CNK1 by Ser22 phosphorylation. CNK1-S22F found in human tumors is a gain-of-function mutant.