title: The nuclear pore complex: oily spaghetti or gummy bear?
abstract: In this issue, Frey and Görlich (2007) provide new insight into the selective barrier that controls protein traffic through the nuclear pore complex. They show that a single protein domain of the nuclear pore protein Nsp1 can form a hydrogel that allows highly selective access of nuclear transport receptors and their cargos, but rejects other proteins of similar size.
authors: Department of Molecular and Cell Biology, Division of Cell and Developmental Biology, University of California Berkeley, Berkeley, CA 94720-3200, USA. kweis@berkeley.edu
authors: Karsten
authors: K
authors: Weis
mesh_terms: D002135:Calcium-Binding Proteins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D022022:Nuclear Pore / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*; D028861:Nuclear Pore Complex Proteins; D009687:Nuclear Proteins / Q000737:chemistry / Q000378:metabolism; D021381:Protein Transport / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D002135:Calcium-Binding Proteins; C062748:NSP1 protein, S cerevisiae; D028861:Nuclear Pore Complex Proteins; D009687:Nuclear Proteins; D029701:Saccharomyces cerevisiae Proteins