Ubiquitins are essentially molecular tags that are found everywhere in the cell.
On the other hand, ubiquitins have a subtle trick up their sleeves - they can tag other tags.
NF-kB activity increases when TRAF3 has the homing targets, called ubiquitins, attached to it and is destroyed by the proteasome, a complex of proteins that hunts down ubiquitin-decorated proteins.
When TRAF3 evades attack, it turns that same destructive mechanism against NIK, a protein that is central to NF-kB activity, by tagging it with ubiquitins.
SMD simulations (17) qualitatively reproduced the differences between these mechanical unfolding patterns and additionally showed, that the major unfolding barrier of extension by force for both C-to-N linked and C-to-Lys 48 linked ubiquitin
was formed by the rupture of hydrogen bonds between specific [beta]-strands: two parallel [beta]-strands (I and V) in C-to-N linked ubiquitin
and two antiparallel [beta]-strands (III and V) in C-to-Lys 48 linked ubiquitins
The researchers showed that KEAP1, short for the tongue-twisting Kelch-like ECH-associated protein 1, binds to IKKB and attaches molecules known as ubiquitins
to the oncoprotein, which targets it for dissolution by the cell's proteasome complex.
are small regulatory proteins that attach to other target proteins allowing their destruction and recycling.
By attaching a string of targeting proteins known as ubiquitins
to the phosphorylated tumor suppressor, MDM2 marks it for destruction by the ubiquitin
-proteasome degradation pathway.