Differential transcription of the first exon of the agrin gene results either in a secreted form that binds to the basal lamina via its laminin-binding N-terminal NtA domain or a shorter isoform without the NtA domain that remains attached to the cellular plasma membrane as a type-II transmembrane protein.
Differential transcription of the first exon results in a longer form which is secreted and binds to the basal lamina via its laminin-binding N-terminal agrin (NtA) domain [11], [16], [17] and a shorter isoform which lacks the NtA domain and remains in the membrane as a type II transmembrane protein [18], [19].
For example, p53 binds to the basal transcription and nucleotide-excision repair complex, TFIIH, through interaction with two DNA helicases, XPB and XPD, and cells with p53 inactivation have a reduced DNA repair activity.
Moderately active AFPs such as Type III AFP (and Type III AFP-GFP) have been shown to bind to the ice basal planes, with the low activity LpAFP binding to the prism planes [19], [20].
This function requires specific interactions that are mediated by integrins through specialized protein domains of the basal membrane compartment, which bind to the corresponding components of extracellular matrix, activating binding of the intracellular domain of integrin to the cytoskeleton via adapter proteins [38], [62], [63].
In chickens, MAL-I bind to the surface of ciliated cells and basal cells, but not goblet cells.
As the p105 gene is activated by NF- κB, this factor can also bind to the p105 promoter and activate the transcription above the basal level.
It can bind to the TATA box, interacts with TFIIA and TFIIB and promotes basal transcription in vitro [ 84, 85].
In the absence of poly(U), a basal level of ternary complex will bind to the ribosome [ 20].
