LAMTOR5
Function
As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids (PubMed:22980980, PubMed:29158492, PubMed:30181260). Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator plays a dual role for the small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD): it (1) acts as a guanine nucleotide exchange factor (GEF), activating the small GTPases Rag and (2) mediates recruitment of Rag GTPases to the lysosome membrane (PubMed:22980980, PubMed:28935770, PubMed:29107538, PubMed:29158492, PubMed:30181260). Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated (PubMed:22980980, PubMed:29158492, PubMed:30181260). When complexed to BIRC5, interferes with apoptosome assembly, preventing recruitment of pro-caspase-9 to oligomerized APAF1, thereby selectively suppressing apoptosis initiated via the mitochondrial/cytochrome c pathway (PubMed:12773388).
Sequence Similarities
Belongs to the LAMTOR5 family.
Tissue Specificity
Highly expressed in skeletal and cardiac muscle, followed by pancreas, kidney, liver, brain, placenta and lung (PubMed:9499022). Elevated levels in both cancerous and non-cancerous liver tissue of patients with chronic HBV infection compared with hepatic tissue without HBV infection (PubMed:9499022).
Cellular localization
- Lysosome
- Cytoplasm
- Cytosol
Alternative names
HBXIP, XIP, LAMTOR5, Ragulator complex protein LAMTOR5, Hepatitis B virus X-interacting protein, Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5, HBV X-interacting protein, HBX-interacting protein