Table 1.

EPLIN-associated molecules

EPLIN association	Biological significance and reference	References
Actin	Actin is an abundant protein important for cell migration. EPLIN has two actin-binding domains that flank the EPLIN LIM domain. Pull-down assays revealed that EPLIN binds actin monomers, and this results in actin cross linking and actin filament bundle assembly.	[15]
Paxillin	May form a complex with EPLIN to co-ordinate actin dynamics. IHC of PCa tissue vs normal reveals that EPLIN overexpression influences paxillin expression and localisation. Co-localisation, co-precipitation and an in situ proximal ligation assay revealed direct association between the two molecules in cultured human mesangial cells.	[12, 13, 16]
α-Catenin	Immunoprecipitation and GST pull-down assays reveal that EPLIN interacts with α-catenin, forming a cadherin–β-catenin–α-catenin–EPLIN complex.	[17]
Supervillin	In vivo co-localisation studies and in vitro GST pull-down assays reveal that EPLIN interacts with the peripheral membrane protein, supervillain.	[18]
PINCH-1	Pull-down assays reveal that endogenous EPLIN co-immunoprecipitates with endogenous PINCH-1 in keratinocytes.	[19]
ERK	ERK phosphorylates EPLIN and decreases EPLIN affinity to F-actin promoting cell migration. Inhibition of ERK abolishes EPLIN expression and reduces tumour-suppressive ability of EPLIN.	[10, 13, 20]
DNp73	In melanoma cells, both EPLIN isoforms are inhibited by DNp73, and this drives a more invasive phenotype.	[21]
SATB2	EPLIN is differentially regulated by the DNA-binding protein, SATB2. SATB2 regulates the actin cytoskeleton via EPLIN association. When SATB2 is knocked out, osteosarcoma cells show reduced migration and are less invasive, and this is mediated by EPLIN.	[22]
Cav-1	EPLIN regulates the lipid raft tumour-suppressive protein, Cav-1. Co-immunoprecipitation and mass spectroscopy analysis revealed that EPLIN and Cav-1 bind to each other in normal and RasV12 cells.	[23]