Table 1.

Binding partners of Nm23-1 H1 and proposed biological consequences

Binding partners	Biological consequences	References
A. Cellular
h-prune	Increases h-prune phosphodiesterase activity and cell motility. Directly correlates with high expression of h-prune and low expression of Nm23-H1 in aggressive tumor cells.	[53,55,56]
STRAP	Negative regulation of TGF-β mediated signaling, Increases p53 activity.	[51,52]
KSR	Direct substrate for histidine kinase activity of Nm23-H1, regulates cell motility by controlling Ras-Raf-MEK-Erk pathway.	[38]
SET	Formation of an inhibitory SET complex, blocks Nm23-H1 mediated exonuclease and tumor metastatic activity.	[43,47,62]
Rad	Maintains GDP-GTP cycling, acts as a GTPase-activating protein for Rad.	[61,168]
Tiaml	Blocks Tiam1-Rac1 mediated signaling pathway, decrease cell motility and intercellular adhesion.	[58]
Dbl-1	Interaction results in loss of Dbl-1 function as a guanine nucleotide exchange factor for Cdc42, and blocks Nm23-H1 activity.	[59]
ERα	Alters estrogen-responsive gene expression.	[60]
B. Viral
EBNA3C	Promotes Nm23-H1 nuclear localization, negatively regulates the metastatic potential of Nm23-H1; together EBNA3C and Nm23-H1 can block Necdin-mediated transcriptional repression and anti- angiogenic activities. In cooperation with Nm23-H1, EBNA3C can transcriptionally upregulate MMP-9, Cox-2 and α-V integrin expression levels.	[13,63,106,107,125,136,148]
EBNA1	Modulates Nm23-H1 associated metastatic activities	[13,105]
LANA	Induces Nm23-H1 nuclear translocation, re-expression of Nm23-H1 blocks KSHV induced cell invasiveness through inhibiting MAPK- signaling pathway.	[167]
E7	Blocks granzyme A-induced apoptosis and promotes cell invasiveness by inhibiting Nm23-H1 multidirectional activities.	[157]