Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Publication

Protor-2 interacts with tristetraprolin to regulate mRNA stability during stress.

Holmes B, Artinian N, Anderson L, Martin J, Masri J, Cloninger C, Bernath A, Bashir T, Benavides-Serrato A, Gera J

The A/U-rich RNA-binding protein tristetraprolin (TTP) is an mRNA destabilizing factor which plays a role in the regulated turnover of many transcripts encoding proteins involved in immune function and cell growth control. TTP also plays a role in stress-induced destabilization of mRNAs. Here we report the interaction of TTP with a component of the mTORC2 kinase, Protor-2 (PRR5-L, protein Q6MZQ0/FLJ14213/CAE45978). ... [more]

Cell. Signal. Jan. 01, 2012; 24(1);309-15 [Pubmed: 21964062]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
ZFP36 DCP1B	Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods.	Youn JY (2018)	Low	-	BioGRID	2817637

Curated By

BioGRID

Interaction Summary

ZFP36

Gene Ontology Biological Process

Gene Ontology Molecular Function

14-3-3 protein binding [IDA]AU-rich element binding [IDA, IMP]C-C chemokine binding [IPI]mRNA binding [IDA]poly(A) RNA binding [IDA]protein binding [IPI]protein kinase binding [IPI]single-stranded RNA binding [TAS]

Gene Ontology Cellular Component

DCP1B