Cytosolic arginine sensor for mTORC1 subunit 1/2, ACT-like
This domain is found in Cytosolic arginine sensor for mTORC1 subunit 1 from humans (CASTOR1) and in similar proteins predominantly from vertebrates. CASTOR1 functions as an intracellular arginine sensor within the amino acid-sensing branch of the TOR ...
This domain is found in Cytosolic arginine sensor for mTORC1 subunit 1 from humans (CASTOR1) and in similar proteins predominantly from vertebrates. CASTOR1 functions as an intracellular arginine sensor within the amino acid-sensing branch of the TORC1 signaling pathway. This entry represents the third out of the four tandem ACT domains present in this protein. This domain adopts the typical beta-alpha- beta-beta-alpha-beta configuration of the ACT domain, although it lacks the last beta-strand. It folds together with the first ACT domain to form an eight-stranded beta-sheet flanked by four alpha- helices on one side, making up the dimerization domain [1,4].
Cytosolic arginine sensor for mTORC1 subunit 1 N-terminal domain
CASTOR1 (Cytosolic arginine sensor for mTORC1 subunit 1) has been identified as the cytosolic arginine sensor for the mTORC1 pathway. In the absence of arginine, CASTOR1 binds to GATOR2 and inhibits mTORC1 signaling; whereas in the presence of argini ...
CASTOR1 (Cytosolic arginine sensor for mTORC1 subunit 1) has been identified as the cytosolic arginine sensor for the mTORC1 pathway. In the absence of arginine, CASTOR1 binds to GATOR2 and inhibits mTORC1 signaling; whereas in the presence of arginine, CASTOR1 interacts with arginine and no longer associates with GATOR2. The arginine sits in a pocket between the N-terminal domain (NTD) and the C-terminal domain (CTD) of CASTOR1. The CASTOR1-NTD on the opposite side of the arginine-binding site was identified to mediate direct physical interaction with its downstream effector GATOR2, via GATOR2 subunit Mios [1].
The ACT domain is a structural motif of 70-90 amino acids that functions in the control of metabolism, solute transport and signal transduction. They are thus found in a variety of different proteins in a variety of different arrangements [1]. In mam ...
The ACT domain is a structural motif of 70-90 amino acids that functions in the control of metabolism, solute transport and signal transduction. They are thus found in a variety of different proteins in a variety of different arrangements [1]. In mammalian phenylalanine hydroxylase the domain forms no contacts but promotes an allosteric effect despite the apparent lack of ligand binding [2].
