In vitro Reconstitution of a Membrane Switch Mechanism for the Polarity Protein LGL

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• 作者：Ilaria Visco¹ ; ^&dagger ; ; ³ ; ^{ilaria.visco@mpi-dortmund.mpg.de} ; Carsten Hoege² ; ^&dagger ; ; Anthony A. Hyman² ; Petra Schwille¹ ; ^{schwille@biochem.mpg.de}
• 关键词：aPKC ; atypical protein kinase C ; bPI(4 ; 5)P2 ; L-α-phosphatidylinositol-4 ; 5-bisphosphate ; BSA ; bovine serum albumin ; DGS-NTA(Ni) ; 1 ; 2-di-(9Z-octadecenoyl)-sn-glycero-3-[(N-(5-amino-1-carboxypentyl)iminodiacetic acid)succinyl] ; DLS ; dynamic light scattering ; DOPC ; 1 ; 2-dioleoyl-sn-glycero-3-phosphocholine ; DOPS ; 1 ; 2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine ; eGFP ; enhanced green fluorescent protein ; GFP ; green fluorescent protein ; GUV ; giant unilamellar vesicle ; His6 ; hexahistidine tag ; LUV
• 刊名：Journal of Molecular Biology
• 出版年：2016
• 出版时间：4 December 2016
• 年：2016
• 卷：428
• 期：24
• 页码：4828-4842
• 全文大小：1521 K
• 卷排序：428

文摘

Lethal giant larvae 1 (LGL-1) binds to negatively charged phospholipids through specific basic residues of a membrane binding sequence. LGL-1 membrane binding induces the formation of an alpha-helix in the membrane binding sequence. Reconstitution of LGL-1 phosphorylation in giant unilamellar vesicles by atypical protein kinase C LGL-1 residues required for membrane binding are required for localization and cell polarity in vivo.