一种粘着斑蛋白zyxin与人乳头瘤病毒6型的E6蛋白相互作用，导致其核转位。
Interaction of zyxin, a focal adhesion protein, with the e6 protein from human papillomavirus type 6 results in its nuclear translocation.
作者信息
Degenhardt Y Y, Silverstein S
机构信息
Department of Pharmacology, College of Physicians and Surgeons, Columbia University, New York, New York 10032, USA.
出版信息
J Virol. 2001 Dec;75(23):11791-802. doi: 10.1128/JVI.75.23.11791-11802.2001.
Abstract
Zyxin, a focal adhesion molecule, interacts specifically with the E6 protein from human papillomavirus (HPV) type 6 in a yeast two-hybrid screen of a cDNA library prepared from human keratinocytes. Zyxin does not interact significantly with E6 proteins from HPV types 11, 16, or 18. The interaction was confirmed by in vitro and in vivo analyses and it requires the LIM domains (Lin-11, Isl-1, and Mec-3 [G. Freyd, S. K. Kim, and H. R. Horvitz, Nature 344:876-879, 1990]) found at the carboxyl terminus of zyxin. Cotransfection of E6 from HPV ((6)E6) and zyxin results in the accumulation of zyxin in the nucleus where it can function as a transcriptional activator. (6)E6 can also mobilize endogenous zyxin to the nucleus.
摘要
斑联蛋白是一种粘着斑分子，在用人角质形成细胞制备的cDNA文库进行的酵母双杂交筛选中，它与人乳头瘤病毒（HPV）6型的E6蛋白特异性相互作用。斑联蛋白与HPV 11、16或18型的E6蛋白无明显相互作用。通过体外和体内分析证实了这种相互作用，并且它需要斑联蛋白羧基末端的LIM结构域（Lin-11、Isl-1和Mec-3 [G. Freyd，S. K. Kim，和H. R. Horvitz，《自然》344:876 - 879，1990]）。HPV 6型的E6（(6)E6）与斑联蛋白共转染导致斑联蛋白在细胞核中积累，在那里它可以作为转录激活因子发挥作用。(6)E6还能将内源性斑联蛋白转运到细胞核。
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