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.

Publication

Exportin-1 functions as an adaptor for transcription factor-mediated docking of chromatin at the nuclear pore complex.

Ge T, Brickner DG, Zehr K, VanBelzen DJ, Zhang W, Caffalette C, Moeller GC, Ungerleider S, Marcou N, Jacob A, Nguyen VQ, Chait B, Rout MP, Brickner JH

Nuclear pore proteins (nucleoporins [Nups]) physically interact with hundreds of chromosomal sites, impacting transcription. In yeast, transcription factors mediate interactions between Nups and enhancers and promoters. To define the molecular basis of this mechanism, we exploited a separation-of-function mutation in the Gcn4 transcription factor that blocks its interaction with the nuclear pore complex (NPC). This mutation reduces the interaction of ... [more]

Mol Cell Mar. 20, 2025; 85(6);1101-1116.e8 [Pubmed: 40068679]

Throughput

High Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
CRM1 RPS13	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.	Kirli K (2015)	High	-	BioGRID	1440288
RPS13 CRM1	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.	Roessler I (2019)	High	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

CRM1

Gene Ontology Biological Process

Gene Ontology Molecular Function

protein transporter activity [IDA, IMP]

Gene Ontology Cellular Component

RPS13