These proteins are collectively known as the shelterin complex or telosome, and they mediate the capping function of the telomere along with telomere length regulation (Blackburn 2001; de Lange 2005).
The formation of Ag(shell)–Au(core) nanoparticles by the reduction of Ag+ ions on preformed Au NPs, mediated by the capping agents like dodecylamine is described.
Initiation of translation of the majority of the eukaryotic cellular mRNAs is mediated by the cap-dependent mode of translation which results from binding of ribosomes to the m7G cap at the 5' end of the mRNA followed by linear scanning to the initiation codon [1].
The proliferation arrest observed in our study might be mediated by disrupting the capping ability of telomerase, thus exposing the telomeres with no protection, leading to proliferation arrest.
Moreover, neogenin mediates netrin-dependent cell clustering, further indicating that netrin-neogenin interactions stabilize the cap cell layer and mediate its adhesion to the preluminal body cells.
Further characterization of this model, particularly in a setting of androgen deprivation, should allow further insight into the mechanisms by which the Tp53 R270H mutation mediates CaP progression.
The cap protects transcripts from exonucleases and recruits complexes which mediate transcription elongation, processing and translation initiation.
The 5′-cap and poly(A) tail stimulate translation synergistically which is mediated by a physical interaction between PABP bound to the poly(A) tail and the cap binding complex [ 8- 11].
The cap structure protects transcripts from exonucleases and recruits complexes, including CBC (cap-binding complex) and eIF4F (eukaryotic initiation factor 4F) complex, which mediate transcription elongation, splicing, nuclear export and translation initiation [ 1].
