Anti-DEPDC5 / DEP domain-containing protein 5

In 1X PBS, pH 7.4, with 0.09% sodium azide. The DEPDC5 gene encodes DEP domain-containing protein 5, a protein which contains a DEP (disheveled, EGL-10, pleckstrin) domain. This domain is known for its involvement in signal transduction and cellular communication, highlighting the importance of DEPDC5 in coordinating crucial cellular processes. DEP domain-containing protein 5 has been implicated in the regulation of cellular signaling pathways, including the mechanistic target of rapamycin complex 1 (mTORC1) pathway. By interacting with key proteins in this pathway, DEPDC5 plays a critical role in maintaining cellular homeostasis and growth. Mutations in the DEPDC5 gene have been linked to various neurological disorders, including familial focal epilepsy. Protein function: As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the mTORC1 pathway (PubMed:23723238, PubMed:25457612, PubMed:29590090, PubMed:29769719, PubMed:31548394, PubMed:35338845). In response to amino acid depletion, the GATOR1 complex has GTPase activating protein (GAP) activity and strongly increases GTP hydrolysis by RagA/RRAGA (or RagB/RRAGB) within heterodimeric Rag complexes, thereby turning them into their inactive GDP-bound form, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling (PubMed:23723238, PubMed:25457612, PubMed:29590090, PubMed:29769719, PubMed:35338845). In the presence of abundant amino acids, the GATOR1 complex is negatively regulated by GATOR2, the other GATOR subcomplex, in this amino acid-sensing branch of the TORC1 pathway (PubMed:23723238, PubMed:25457612, PubMed:29769719). Within the GATOR1 complex, DEPDC5 mediates direct interaction with the nucleotide- binding pocket of small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD) and coordinates their nucleotide loading states by promoting RagA/RRAGA or RagB/RRAGB into their GDP-binding state and RagC/RRAGC or RagD/RRAGD into their GTP-binding state (PubMed:29590090, PubMed:35338845). However, it does not execute the GAP activity, which is mediated by NPRL2 (PubMed:29590090). [The UniProt Consortium]