Abstract
The mechanistic target of rapamycin (mTORC1) is an expert cell production
controller which reacts to a different set of natural information sources, such as amino
acids. Various proteins have been differentiated recently to help communicate amino
acid accessibility to mTORC1. Rag guanosine triphosphatases (GTPases) transfer
amino acid accessibility to the mTORC1 duct, and the mTORC1 apprentice to the
amino acid on the Lysosome in a conventional manner. Later on, several sensors were
exposed for the amino acid-reinforced mTORC1 pathway, including Leucine, Argina,
and S-adenosyl methionine. The representation of these sensors is essential to explain
why cells change the pathways of amino acid detection requirements. Here, we survey
these new advances and feature the assortment of further inquiries that rise out of the
recognizable proof of these sensors.