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Bad is a member of the Bcl2 family and acts to promote apoptosis by forming heterodimers with the survival proteins Bcl2 and BclxL, thus preventing them from binding with BAX. Bad is found on the outer mitochondrial membrane and, once phosphorylated in response to growth stimuli, translocates to the cytoplasm. The phosphorylation status of Bad represents a key checkpoint for death or cell survival. JNK-induced phosphorylation of BAD serine 128 promotes the apoptotic role of Bad by opposing th

This gene encodes a member of the aurora kinase subfamily of serine/threonine kinases. The genes encoding the other two members of this subfamily are located on chromsomes 19 and 20. These kinases participate in the regulation of segregation of chromosomes during mitosis and meiosis through association with microtubules. A pseudogene of this gene is located on chromosome 8. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Feb 2012].

Aurora A plays a role in cell cycle regulation during anaphase and/or telophase, in relation to the function of the centrosome/spindle pole region during chromosome segregation. Aurora A plays a key role during tumor development and progression and is overexpressed in many human cancers including breast, ovarian and colorectal. Aurora A is viewed as a potential target for anticancer drug treatment.$n$nAurora B is a mitotic protein kinase that phosphorylates histone H3 (probably on Serine 10)

This gene encodes a member of the human ARF gene family, which is part of the RAS superfamily. The ARF genes encode small guanine nucleotide-binding proteins that stimulate the ADP-ribosyltransferase activity of cholera toxin and play a role in vesicular trafficking and as activators of phospholipase D. The product of this gene is localized to the plasma membrane, and regulates vesicular trafficking, remodelling of membrane lipids, and signaling pathways that lead to actin remodeling. A pse

GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking among different compartments. Modulates vesicle budding and uncoating within the Golgi complex. Deactivation induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, suggesting a crucial role in protein trafficking. In its GTP-bound form, its triggers the association with coat proteins with the Golgi membran

The RAF family of signaling proteins has three isoforms: A RAF, RAF 1 and B RAF. These proteins are instrumental in forwarding the stimulus generated by mitogens from monomeric G proteins to the MAP kinase pathway. RAF 1 is known to be downstream of Ras and binds to it by an N terminal noncatalytic domain. This domain is conserved in A RAF and B RAF. 14-3-3 is also known to be an activator of RAFs. Activated RAF directly phosphorylates and activates MEK. A RAF is expressed at a very high co