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 LIM/double zinc-finger motif functions as a protein dimerization domain.

Feuerstein R, Wang X, Song D, Cooke NE, Liebhaber SA

Protein-protein interactions resulting in dimerization and heterodimerization are of central importance in the control of gene expression and cell function. Proteins that share the 52-residue LIM/double zinc-finger domain are involved in a wide range of developmental and cellular controls. Some of these functions have been hypothesized to involve protein dimerization. In the present report we demonstrate, using both in vitro ... [more]

Proc. Natl. Acad. Sci. U.S.A. Oct. 25, 1994; 91(22);10655-9 [Pubmed: 7938009]

Throughput

Low Throughput

Related interactions

Interaction	Experimental Evidence Code	Dataset	Throughput	Score	Curated By	Notes
CSRP1 CSRP1	Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.	Feuerstein R (1994)	Low	-	BioGRID	-

Curated By

BioGRID

Interaction Summary

CSRP1

Gene Ontology Biological Process

Gene Ontology Molecular Function

poly(A) RNA binding [IDA]

Gene Ontology Cellular Component