IKBKAP

[1] The IKAP protein is thought to participate as a sub-unit in the assembly of a six-protein putative human holo-Elongator complex,[2] which allows for transcriptional elongation by RNA polymerase II.

[3] Other pathways that have been connected to IKAP protein function in a variety of organisms include tRNA modification,[citation needed] cell motility,[4] and cytosolic stress signalling.

In an in vivo experiment, researchers showed direct interaction between IKAP and JNK induced by the application of stressors such as ultraviolet light and TNF-α (a pro-inflammatory cytokine).

[9] The association of the elongator complex with RNA polymerase II holoenzyme is necessary for subsequent binding to nascent pre-mRNA of certain target genes, and thus their successful transcription.

Familial dysautonomia (also known as “Riley-Day syndrome”) is a complex congenital neurodevelopmental disease, characterized by unusually low numbers of neurons in the sensory and autonomic nervous systems.

[3] The single-base mutation, overwhelmingly noted as a transition from cytosine to thymine, is present in the 5’ splice donor site of intron 20 in the IKBKAP pre-mRNA.

In contrast, brain tissue with the single-base mutation in the IKBKAP gene predominantly express a resulting truncated, mutant IKAP protein which is nonfunctional.

[4] In a small number of reported familial dysautonomia cases, researchers have identified other mutations that cause a change in amino acids (the building blocks of proteins).