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Gene Review

NUP53  -  Nup53p

Saccharomyces cerevisiae S288c

Synonyms: Nuclear pore protein NUP53, Nucleoporin NUP53, YM8520.02, YMR153W
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High impact information on NUP53

  • These changes allow a transport inhibitory nucleoporin, Nup53p, to bind the karyopherin Kap121p specifically during mitosis, slowing its movement through the NPC and inducing cargo release [1].
  • Accompanying these events is the Nup53p-dependent hyperphosphorylation of Mad1p [2].
  • By altering the expression of a single nucleoporin gene, NUP53, we showed that the overproduction of Nup53p altered nuclear transport and had a profound effect on the structure of the nuclear membrane [3].
  • We also demonstrated that the targeting of excess Nup53p to the NPC and its specific association with intranuclear membranes were dependent on the karyopherin Kap121p and the nucleoporin Nup170p [3].
  • At the nuclear envelope, the abilities of Nup53p to associate with the membrane and drive membrane proliferation were dependent on a COOH-terminal segment containing a potential amphipathic alpha-helix [3].

Biological context of NUP53


Anatomical context of NUP53

  • Here, Nup53p induced the formation of intranuclear, tubular membranes that later formed flattened, double membrane lamellae structurally similar to the nuclear envelope [3].
  • Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex [6].

Physical interactions of NUP53


Other interactions of NUP53

  • Kap121p can be released from Nup53p by the GTP bound form of the small GTPase Ran [4].
  • By doing so, we identified the yeast nucleoporin Nup53p, which also exhibits multiple locations within the yeast NPC and colocalizes with Nic96p in all its locations [7].
  • Whereas Nup53p is directly involved in NLS-mediated protein import by its interaction with the yeast nuclear import receptor Kap95p, it appears not to participate in NES-dependent nuclear export [7].

Analytical, diagnostic and therapeutic context of NUP53


  1. Cell cycle regulated transport controlled by alterations in the nuclear pore complex. Makhnevych, T., Lusk, C.P., Anderson, A.M., Aitchison, J.D., Wozniak, R.W. Cell (2003) [Pubmed]
  2. The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint. Iouk, T., Kerscher, O., Scott, R.J., Basrai, M.A., Wozniak, R.W. J. Cell Biol. (2002) [Pubmed]
  3. A link between the synthesis of nucleoporins and the biogenesis of the nuclear envelope. Marelli, M., Lusk, C.P., Chan, H., Aitchison, J.D., Wozniak, R.W. J. Cell Biol. (2001) [Pubmed]
  4. Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p. Marelli, M., Aitchison, J.D., Wozniak, R.W. J. Cell Biol. (1998) [Pubmed]
  5. Karyopherins in nuclear pore biogenesis: a role for Kap121p in the assembly of Nup53p into nuclear pore complexes. Lusk, C.P., Makhnevych, T., Marelli, M., Aitchison, J.D., Wozniak, R.W. J. Cell Biol. (2002) [Pubmed]
  6. Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex. Hawryluk-Gara, L.A., Shibuya, E.K., Wozniak, R.W. Mol. Biol. Cell (2005) [Pubmed]
  7. The yeast nucleoporin Nup53p specifically interacts with Nic96p and is directly involved in nuclear protein import. Fahrenkrog, B., Hübner, W., Mandinova, A., Panté, N., Keller, W., Aebi, U. Mol. Biol. Cell (2000) [Pubmed]
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