High impact information on NUP145

• A stretch of 140 amino acids within Nup145p is conserved in two other yeast nucleoporins, Nup116p and Nup100p, and in an uncharacterized C. elegans protein [1].
• An essential yeast protein, Nup145p, is identified via its genetic interaction with the nucleoporin Nsp1p [1].
• Nup145p contains GLFG repeats and localizes to nuclear pores [1].
• Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif [1].
• This biogenesis pathway for Nup98 and Nup96 is evolutionarily conserved, as the putative Saccharomyces cerevisiae homologues, N-Nup145p and C-Nup145p, are also produced through proteolytic cleavage of a precursor protein [2].

Biological context of NUP145

• This phenotype is similar to that previously observed in the disruption of another nucleoporin gene, NUP145 [3].
• Two functionally distinct domains generated by in vivo cleavage of Nup145p: a novel biogenesis pathway for nucleoporins [4].

Anatomical context of NUP145

• NUP145 encodes a novel yeast glycine-leucine-phenylalanine-glycine (GLFG) nucleoporin required for nuclear envelope structure [5].

Associations of NUP145 with chemical compounds

• In this study, the proteolytic cleavage site of Nup145p has been mapped upstream of an evolutionary conserved serine residue [6].

Physical interactions of NUP145

• We have additionally shown that a peptide from the N terminus of the nucleoporin Nup145p-C binds Nup116p-C [7].

Other interactions of NUP145

• Strains mutant for Nup49p or Nup116p, or genetically depleted of Nup145p, strongly accumulated unspliced pre-tRNAs [8].
• However, the N-Nup145p becomes essential in a nup188 mutant background [4].

Analytical, diagnostic and therapeutic context of NUP145

• Thin section electron microscopy analysis revealed the presence of what appeared to be successive herniations of the nuclear envelope forming grape-like structures at primarily one site on the nup145 delta N nuclei [5].

References