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.

Publication

The Coxsackievirus and adenovirus receptor (CAR) forms a complex with the PDZ domain-containing protein ligand-of-numb protein-X (LNX).

Sollerbrant K, Raschperger E, Mirza M, Engstrom U, Philipson L, Ljungdahl PO, Pettersson RF

The Coxsackievirus and adenovirus receptor (CAR) functions as a virus receptor, but its primary biological function is unknown. A yeast two-hybrid screen was used to identify Ligand-of-Numb protein-X (LNX) as a binding partner to the intracellular tail of CAR. LNX harbors several protein-protein interacting domains, including four PDZ domains, and was previously shown to bind to and regulate the expression ... [more]

J. Biol. Chem. Feb. 28, 2003; 278(9);7439-44 [Pubmed: 12468544]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
CAR1 LNX1	Two-hybrid Two-hybrid 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.	Sollerbrant K (2003)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

CAR1

Gene Ontology Cellular Component

LNX1

Gene Ontology Biological Process

Gene Ontology Molecular Function

PDZ domain binding [IDA]protein binding [IPI]ubiquitin-protein transferase activity [IDA]