BioPlex Interactome

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SAMTOR is an S-adenosylmethionine sensor for the mTORC1 pathway

Gu et al. describe a potential molecular link between the effects of methionine restriction and the growth controller mTOR complex 1 (mTORC1), a well-validated regulator of life span and health span in many organisms. They identify a protein that they named SAMTOR as a component of the nutrient-sensing pathway upstream of mTORC1.

The CASTOR Proteins Are Arginine Sensors for the mTORC1 Pathway

Here, we show that CASTOR1, a previously uncharacterized protein, interacts with GATOR2 and is required for arginine deprivation to inhibit mTORC1. CASTOR1 homodimerizes and can also heterodimerize with the related protein, CASTOR2. Arginine disrupts the CASTOR1-GATOR2 complex by binding to CASTOR1 with a dissociation constant of ∼30 μM, and its arginine-binding capacity is required for arginine to activate mTORC1 in cells.

Integration of over 9,000 mass spectrometry experiments builds a global map of human protein complexes

Here, through the synthesis of over 9,000 published mass spectrometry experiments, we present hu.MAP, the most comprehensive and accurate human protein complex map to date, containing > 4,600 total complexes, > 7,700 proteins, and > 56,000 unique interactions, including thousands of confident protein interactions not identified by the original publications.