Passa al contenuto
Merck

The TORC1 phosphoproteome in C. elegans reveals roles in transcription and autophagy.

iScience (2022-04-29)
Aileen K Sewell, Zachary C Poss, Christopher C Ebmeier, Jeremy R Jacobsen, William M Old, Min Han
ABSTRACT

The protein kinase complex target of rapamycin complex 1 (TORC1) is a critical mediator of nutrient sensing that has been widely studied in cultured cells and yeast, yet our understanding of the regulatory activities of TORC1 in the context of a whole, multi-cellular organism is still very limited. Using Caenorhabditis elegans, we analyzed the DAF-15/Raptor-dependent phosphoproteome by quantitative mass spectrometry and characterized direct kinase targets by in vitro kinase assays. Here, we show new targets of TORC1 that indicate previously unknown regulation of transcription and autophagy. Our results further show that DAF-15/Raptor is differentially expressed during postembryonic development, suggesting a dynamic role for TORC1 signaling throughout the life span. This study provides a comprehensive view of the TORC1 phosphoproteome, reveals more than 100 DAF-15/Raptor-dependent phosphosites that reflect the complex function of TORC1 in a whole, multi-cellular organism, and serves as a rich resource to the field.

MATERIALI
N° Catalogo
Marchio
Descrizione del prodotto

Sigma-Aldrich
Anti-actina, affinity isolated antibody, buffered aqueous solution
Sigma-Aldrich
AptaFluor® SAH Methyltransferase Assay