BAIT

NUP116

NSP116, FG-nucleoporin NUP116, L000001293, YMR047C
FG-nucleoporin component of central core of the nuclear pore complex; contributes directly to nucleocytoplasmic transport and maintenance of the nuclear pore complex (NPC) permeability barrier; forms a stable association with Nup82p, Gle2p and two other FG-nucleoporins (Nsp1p and Nup159p); NUP116 has a paralog, NUP100, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)
PREY

NUP133

RAT3, L000002620, YKR082W
Subunit of Nup84p subcomplex of nuclear pore complex (NPC); contributes to nucleocytoplasmic transport, NPC biogenesis; is involved in establishment of a normal nucleocytoplasmic concentration gradient of GTPase Gsp1p; also plays roles in several processes that may require localization of genes or chromosomes at nuclear periphery, including double-strand break repair, transcription and chromatin silencing; relocalizes to cytosol in response to hypoxia; homolog of human NUP133
Saccharomyces cerevisiae (S288c)

Synthetic Growth Defect

A genetic interaction is inferred when mutations in separate genes, each of which alone causes a minimal phenotype, result in a significant growth defect under a given condition when combined in the same cell.

Publication

Nuclear envelope-vacuole contacts mitigate nuclear pore complex assembly stress.

Lord CL, Wente SR

The intricacy of nuclear pore complex (NPC) biogenesis imposes risks of failure that can cause defects in nuclear transport and nuclear envelope (NE) morphology; however, cellular mechanisms used to alleviate NPC assembly stress are not well defined. In the budding yeast Saccharomyces cerevisiae, we demonstrate that NVJ1- and MDM1-enriched NE-vacuole contacts increase when NPC assembly is compromised in several nup ... [more]

J Cell Biol Dec. 07, 2019; 219(12); [Pubmed: 33053148]

Throughput

  • Low Throughput

Ontology Terms

  • vegetative growth (APO:0000106)

Additional Notes

  • Figure 2
  • nup116-deltaGLFG

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
NUP133 NUP116
Affinity Capture-MS
Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

Low-BioGRID
-
NUP116 NUP133
Affinity Capture-MS
Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

High-BioGRID
-
NUP116 NUP133
Affinity Capture-MS
Affinity Capture-MS

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.

High-BioGRID
3384855
NUP116 NUP133
Co-purification
Co-purification

An interaction is inferred from the identification of two or more protein subunits in a purified protein complex, as obtained by classical biochemical fractionation or affinity purification and one or more additional fractionation steps.

Low-BioGRID
-
NUP116 NUP133
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.6179BioGRID
2005481
NUP116 NUP133
Reconstituted Complex
Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

High-BioGRID
-

Curated By

  • BioGRID