Petersen J M, Her L S, Varvel V, Lund E, Dahlberg J E
Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706-1532, USA.
Mol Cell Biol. 2000 Nov;20(22):8590-601. doi: 10.1128/MCB.20.22.8590-8601.2000.
The matrix (M) protein of vesicular stomatitis virus (VSV) is a potent inhibitor of bidirectional nuclear transport. Here we demonstrate that inhibition occurs when M protein is in the nucleus of Xenopus laevis oocytes and that M activity is readily reversed by a monoclonal antibody (alphaM). We identify a region of M protein, amino acids 51 to 59, that is required both for inhibition of transport and for efficient recognition by alphaM. When expressed in transfected HeLa cells, M protein colocalizes with nuclear pore complexes (NPCs) at the nuclear rim. Moreover, mutation of a single amino acid, methionine 51, eliminates both transport inhibition and targeting to NPCs. We propose that M protein inhibits bidirectional transport by interacting with a component of the NPC or an NPC-associated factor that participates in nucleocytoplasmic transport.
水泡性口炎病毒（VSV）的基质（M）蛋白是一种双向核转运的有效抑制剂。在此我们证明，当M蛋白存在于非洲爪蟾卵母细胞核中时会发生抑制作用，并且M蛋白的活性可被一种单克隆抗体（αM）轻易逆转。我们鉴定出M蛋白的一个区域，即氨基酸51至59，它对于转运抑制和αM的有效识别均是必需的。当在转染的HeLa细胞中表达时，M蛋白与核边缘的核孔复合体（NPC）共定位。此外，单个氨基酸甲硫氨酸51的突变消除了转运抑制和对NPC的靶向作用。我们提出，M蛋白通过与NPC的一个组分或参与核质转运的NPC相关因子相互作用来抑制双向转运。
