The nuclear pore complex: oily spaghetti or gummy bear?
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.
Weis
Karsten
K
Department of Molecular and Cell Biology, Division of Cell and Developmental Biology, University of California Berkeley, Berkeley, CA 94720-3200, USA. kweis@berkeley.edu
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
D002135:Calcium-Binding Proteins; C062748:NSP1 protein, S cerevisiae; D028861:Nuclear Pore Complex Proteins; D009687:Nuclear Proteins; D029701:Saccharomyces cerevisiae Proteins