BAIT

KCNA3

potassium voltage-gated channel, shaker-related subfamily, member 3
Rattus norvegicus
PREY

MMP23

matrix metallopeptidase 23
GO Process (2)
GO Function (1)
GO Component (0)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Rattus norvegicus

Co-localization

Interaction inferred from two proteins that co-localize in the cell by indirect immunofluorescence only when in addition, if one gene is deleted, the other protein becomes mis-localized. Also includes co-dependent association of proteins with promoter DNA in chromatin immunoprecipitation experiments.

Publication

Intracellular trafficking of the KV1.3 potassium channel is regulated by the prodomain of a matrix metalloprotease.

Nguyen HM, Galea CA, Schmunk G, Smith BJ, Edwards RA, Norton RS, Chandy KG

Matrix metalloproteases (MMPs) are endopeptidases that regulate diverse biological processes. Synthesized as zymogens, MMPs become active after removal of their prodomains. Much is known about the metalloprotease activity of these enzymes, but noncanonical functions are poorly defined, and functions of the prodomains have been largely ignored. Here we report a novel metalloprotease-independent, channel-modulating function for the prodomain of MMP23 (MMP23-PD). ... [more]

J. Biol. Chem. Mar. 01, 2013; 288(9);6451-64 [Pubmed: 23300077]

Throughput

  • Low Throughput

Additional Notes

  • MMP23-FL and MMP23-PD both co-localized significantly with the KV1.2-1.3 chimera, but not with the KV1.3-1.2 chimera

Curated By

  • BioGRID