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

The TRPM7 channel is inactivated by PIP(2) hydrolysis.

Runnels LW, Yue L, Clapham DE

TRPM7 (ChaK1, TRP-PLIK, LTRPC7) is a ubiquitous, calcium-permeant ion channel that is unique in being both an ion channel and a serine/threonine kinase. The kinase domain of TRPM7 directly associates with the C2 domain of phospholipase C (PLC). Here, we show that in native cardiac cells and heterologous expression systems, G alpha q-linked receptors or tyrosine kinase receptors that activate ... [more]

Nat. Cell Biol. May. 01, 2002; 4(5);329-36 [Pubmed: 11941371]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
TRPM7 PLCB2	Affinity Capture-Western Affinity Capture-Western 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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.	Runnels LW (2002)	Low	-	BioGRID	-
TRPM7 PLCB2	Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro.	Runnels LW (2002)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

PLCB2

Gene Ontology Biological Process

Gene Ontology Molecular Function

phospholipase C activity [TAS]

Gene Ontology Cellular Component

TRPM7