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

A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways.

Taipale M, Tucker G, Peng J, Krykbaeva I, Lin ZY, Larsen B, Choi H, Berger B, Gingras AC, Lindquist S

Chaperones are abundant cellular proteins that promote the folding and function of their substrate proteins (clients). InÂ vivo, chaperones also associate with a large and diverse set of cofactors (cochaperones) that regulate their specificity and function. However, how these cochaperones regulate protein folding and whether they have chaperone-independent biological functions is largely unknown. We combined mass spectrometry and quantitative high-throughput LUMIER ... [more]

Cell Jul. 17, 2014; 158(2);434-48 [Pubmed: 25036637]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
HSP90AB1 TMOD4	Affinity Capture-Luminescence Affinity Capture-Luminescence An interaction is inferred when a bait protein, tagged with luciferase, is enzymatically detected in immunoprecipitates of the prey protein as light emission. The prey protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag.	Taipale M (2014)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

HSP90AB1

Gene Ontology Biological Process

Gene Ontology Molecular Function

MHC class II protein complex binding [IDA]TPR domain binding [ISS]double-stranded RNA binding [IDA]kinase binding [IPI]nitric-oxide synthase regulator activity [ISS]poly(A) RNA binding [IDA]protein binding [IPI]

Gene Ontology Cellular Component

TMOD4