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Chromosoma

, Volume 107, Issue 4, pp 228–236 | Cite as

Amino-terminal sequences that direct nucleoporin Nup153 to the inner surface of the nuclear envelope

  • Paul Enarson
  • Mark Enarson
  • Ricardo Bastos
  • Brian Burke
Original articles

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.

Keywords

Pyruvate Zinc Finger Nuclear Envelope Pyruvate Kinase Target Function 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin Heidelberg 1998

Authors and Affiliations

  • Paul Enarson
    • 1
  • Mark Enarson
    • 1
  • Ricardo Bastos
    • 1
  • Brian Burke
    • 1
  1. 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 4N1CA

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