The GLFG repetitive region of the nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factor - PubMed (original) (raw)
The GLFG repetitive region of the nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factor
M K Iovine et al. J Cell Biol. 1995 Dec.
Abstract
Nup116p is a member of a family of five yeast nuclear pore complex (NPC) proteins that share an amino terminal region of repetitive tetrapeptide "GLFG" motifs. Previous experiments characterized the unique morphological perturbations that occur in a nup116 null mutant: temperature-sensitive formation of nuclear envelope seals over the cytoplasmic face of the NPC (Wente, S. R., and G. Blobel. 1993. J. Cell Biol. 123:275-284). Three approaches have been taken to dissect the structural basis for Nup116p's role in NPC function. First, deletion mutagenesis analysis of NUP116 revealed that the GLFG region was required for NPC function. This was not true for the other four yeast GLFG family members (Nup49p, Nup57p, Nup100p, and Nup145p). Moreover, deletion of either half of Nup116p's GLFG repeats or replacement of Nup116p's GLFG region with either Nup100p's GLFG region or Nsp1p's FXFG repetitive region abolishes the function of Nup116p. At a semipermissive growth temperature, the cells lacking Nup116p's GLFG region displayed a diminished capacity for nuclear import. Second, overexpression of Nup116p's GLFG region severely inhibited cell growth, rapidly blocked polyadenylated-RNA export, and fragmented the nucleolus. Although it inhibited nuclear export, the overexpressed GLFG region appeared predominantly localized in the cytoplasm and NPC/nuclear envelope structure was not perturbed in thin section electron micrographs. Finally, using biochemical and two-hybrid analysis, an interaction was characterized between Nup116p's GLFG region and Kap95p, an essential yeast homologue of the vertebrate nuclear import factor p97/Imp90/karopherin beta. These data show that Nup116p's GLFG region has an essential role in mediating nuclear transport.
Similar articles
- The GLFG regions of Nup116p and Nup100p serve as binding sites for both Kap95p and Mex67p at the nuclear pore complex.
Strawn LA, Shen T, Wente SR. Strawn LA, et al. J Biol Chem. 2001 Mar 2;276(9):6445-52. doi: 10.1074/jbc.M008311200. Epub 2000 Dec 4. J Biol Chem. 2001. PMID: 11104765 - Nup116p and nup100p are interchangeable through a conserved motif which constitutes a docking site for the mRNA transport factor gle2p.
Bailer SM, Siniossoglou S, Podtelejnikov A, Hellwig A, Mann M, Hurt E. Bailer SM, et al. EMBO J. 1998 Feb 16;17(4):1107-19. doi: 10.1093/emboj/17.4.1107. EMBO J. 1998. PMID: 9463388 Free PMC article. - The nuclear pore complex.
Hurt EC. Hurt EC. FEBS Lett. 1993 Jun 28;325(1-2):76-80. doi: 10.1016/0014-5793(93)81417-x. FEBS Lett. 1993. PMID: 8513897 Review. - Functions of reticulons in plants: What we can learn from animals and yeasts.
Nziengui H, Schoefs B. Nziengui H, et al. Cell Mol Life Sci. 2009 Feb;66(4):584-95. doi: 10.1007/s00018-008-8373-y. Cell Mol Life Sci. 2009. PMID: 18989623 Free PMC article. Review.
Cited by
- Evolutionary trajectory for nuclear functions of ciliary transport complex proteins.
Ewerling A, May-Simera HL. Ewerling A, et al. Microbiol Mol Biol Rev. 2024 Sep 26;88(3):e0000624. doi: 10.1128/mmbr.00006-24. Epub 2024 Jul 12. Microbiol Mol Biol Rev. 2024. PMID: 38995044 Review. - Barrier properties of Nup98 FG phases ruled by FG motif identity and inter-FG spacer length.
Ng SC, Biswas A, Huyton T, Schünemann J, Reber S, Görlich D. Ng SC, et al. Nat Commun. 2023 Feb 10;14(1):747. doi: 10.1038/s41467-023-36331-4. Nat Commun. 2023. PMID: 36765044 Free PMC article. - A simple thermodynamic description of phase separation of Nup98 FG domains.
Ng SC, Görlich D. Ng SC, et al. Nat Commun. 2022 Oct 18;13(1):6172. doi: 10.1038/s41467-022-33697-9. Nat Commun. 2022. PMID: 36257947 Free PMC article. - Percolation transition prescribes protein size-specific barrier to passive transport through the nuclear pore complex.
Winogradoff D, Chou HY, Maffeo C, Aksimentiev A. Winogradoff D, et al. Nat Commun. 2022 Sep 1;13(1):5138. doi: 10.1038/s41467-022-32857-1. Nat Commun. 2022. PMID: 36050301 Free PMC article. - Using Single Molecule RNA FISH to Determine Nuclear Export and Transcription Phenotypes in Drosophila Tissues.
Aleman JR, Little SC, Capelson M. Aleman JR, et al. Methods Mol Biol. 2022;2502:113-125. doi: 10.1007/978-1-0716-2337-4_8. Methods Mol Biol. 2022. PMID: 35412235 Free PMC article.
References
- Proc Natl Acad Sci U S A. 1995 Jan 3;92(1):225-9 - PubMed
- Cell. 1994 Dec 16;79(6):931-4 - PubMed
- Cell. 1994 Jul 29;78(2):275-89 - PubMed
- J Cell Biol. 1987 May;104(5):1157-64 - PubMed
- Cell. 1990 Jan 12;60(1):17-29 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases