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

The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation.

Bhattacharya K, Weidenauer L, Luengo TM, Pieters EC, Echeverria PC, Bernasconi L, Wider D, Sadian Y, Koopman MB, Villemin M, Bauer C, Ruediger SGD, Quadroni M, Picard D

Hop/Stip1/Sti1 is thought to be essential as a co-chaperone to facilitate substrate transfer between the Hsp70 and Hsp90 molecular chaperones. Despite this proposed key function for protein folding and maturation, it is not essential in a number of eukaryotes and bacteria lack an ortholog. We set out to identify and to characterize its eukaryote-specific function. Human cell lines and the ... [more]

Nat Commun Nov. 25, 2020; 11(1);5975 [Pubmed: 33239621]

Throughput

High Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
STAU1 STIP1	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.	Lee SH (2019)	High	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

STIP1

Gene Ontology Biological Process

Gene Ontology Molecular Function

poly(A) RNA binding [IDA]protein binding [IPI]

Gene Ontology Cellular Component

STAU1