Amino-terminal sequences that direct nucleoporin Nup153 to the inner surface of the nuclear envelope |
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Authors: | Paul Enarson Mark Enarson Ricardo Bastos Brian Burke |
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Institution: | (1) Department of Cell Biology and Anatomy, and Cancer Biology Research Group, Faculty of Medicine, The University of Calgary, 3330 Hospital Drive NW, Calgary AB, Canada T2N 4N1, CA |
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Abstract: | Nup153 is a large O-linked glycoprotein that is a component of the basket-like structure that forms the nucleoplasmic face
of nuclear pore complexes (NPCs). The Nup153 molecule has a tripartite structure consisting of N- and C-terminal domains flanking
a central zinc finger domain. All of the targeting and assembly information contained within Nup153 is contributed by the
N-domain. In fact this region of the molecule can target a cytosolic protein, pyruvate kinase, to the nucleoplasmic face of
the NPC. The zinc finger and C-terminal domains appear to have no role in these targeting and assembly activities. Deletion
analysis reveals that there are two distinct regions within the Nup153 N-domain that contain different targeting functions.
One of these is directly involved in assembly into the NPC while a second overlapping region may target Nup153, as well as
other reporter molecules, to the inner face of the nuclear envelope.
Received: 2 March 1998; in revised form: 4 June 1998 / Accepted: 24 June 1998 |
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Keywords: | |
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