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TitlemTORC1 phosphorylates and stabilizes LST2 to negatively regulate EGFR.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 121, Issue 34, Page e2405959121, Year 2024
Publish dateAug 20, 2024
AuthorsStefania Battaglioni / Louise-Marie Craigie / Sofia Filippini / Timm Maier / Michael N Hall /
PubMed AbstractTORC1 (target of rapamycin complex 1) is a highly conserved protein kinase that plays a central role in regulating cell growth. Given the role of mammalian TORC1 (mTORC1) in metabolism and disease, ...TORC1 (target of rapamycin complex 1) is a highly conserved protein kinase that plays a central role in regulating cell growth. Given the role of mammalian TORC1 (mTORC1) in metabolism and disease, understanding mTORC1 downstream signaling and feedback loops is important. mTORC1 recognizes some of its substrates via a five amino acid binding sequence called the TOR signaling (TOS) motif. mTORC1 binding to a TOS motif facilitates phosphorylation of a distinct, distal site. Here, we show that LST2, also known as ZFYVE28, contains a TOS motif (amino acids 401 to 405) and is directly phosphorylated by mTORC1 at serine 670 (S670). mTORC1-mediated S670 phosphorylation promotes LST2 monoubiquitination on lysine 87 (K87). Monoubiquitinated LST2 is stable and displays a broad reticular distribution. When mTORC1 is inactive, unphosphorylated LST2 is degraded by the proteasome. The absence of LST2 enhances EGFR (epidermal growth factor receptor) signaling. We propose that mTORC1 negatively feeds back on its upstream receptor EGFR via LST2.
External linksProc Natl Acad Sci U S A / PubMed:39141345 / PubMed Central
MethodsEM (single particle)
Resolution3.27 - 4.02 Å
Structure data

50181

9f42

EMDB-50181, PDB-9f42:
cryo-EM structure of LST2 TOS peptide bound to human mTOR complex 1, focused on RAPTOR
Method: EM (single particle) / Resolution: 3.27 Å

50182

9f43

EMDB-50182, PDB-9f43:
cryo-EM structure of human LST2 bound to human mTOR complex 1, focused on RAPTOR
Method: EM (single particle) / Resolution: 3.49 Å

50183

9f44

EMDB-50183, PDB-9f44:
cryo-EM structure of LST2 TOS peptide bound to human mTOR complex 1
Method: EM (single particle) / Resolution: 3.68 Å

50184

9f45

EMDB-50184, PDB-9f45:
cryo-EM structure of human LST2 bound to human mTOR complex 1
Method: EM (single particle) / Resolution: 3.74 Å

EMDB-50253: cryo-EM structure of human LST2 bound to human mTOR complex 1
Method: EM (single particle) / Resolution: 4.02 Å

EMDB-50254: Cryo-EM structure of human LST2 bound to human mTOR complex 1, focused on one protomer
Method: EM (single particle) / Resolution: 3.75 Å

EMDB-50255: Cryo-EM structure of human LST2 bound to human mTOR complex 1, focused on one protomer
Method: EM (single particle) / Resolution: 3.73 Å

Chemicals

ChemComp-IHP:
INOSITOL HEXAKISPHOSPHATE

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / MTOR / MTORC1 / LST2 / ZFYVE28 / EGFR / TOS

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