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TitleRegulation of RAS palmitoyltransferases by accessory proteins and palmitoylation.
Journal, issue, pagesNat Struct Mol Biol, Vol. 31, Issue 3, Page 436-446, Year 2024
Publish dateJan 5, 2024
AuthorsAnlan Yang / Shengjie Liu / Yuqi Zhang / Jia Chen / Yujing Fan / Fengxiang Wang / Yilong Zou / Shan Feng / Jianping Wu / Qi Hu /
PubMed AbstractPalmitoylation of cysteine residues at the C-terminal hypervariable regions in human HRAS and NRAS, which is necessary for RAS signaling, is catalyzed by the acyltransferase DHHC9 in complex with its ...Palmitoylation of cysteine residues at the C-terminal hypervariable regions in human HRAS and NRAS, which is necessary for RAS signaling, is catalyzed by the acyltransferase DHHC9 in complex with its accessory protein GCP16. The molecular basis for the acyltransferase activity and the regulation of DHHC9 by GCP16 is not clear. Here we report the cryo-electron microscopy structures of the human DHHC9-GCP16 complex and its yeast counterpart-the Erf2-Erf4 complex, demonstrating that GCP16 and Erf4 are not directly involved in the catalytic process but stabilize the architecture of DHHC9 and Erf2, respectively. We found that a phospholipid binding to an arginine-rich region of DHHC9 and palmitoylation on three residues (C24, C25 and C288) were essential for the catalytic activity of the DHHC9-GCP16 complex. Moreover, we showed that GCP16 also formed complexes with DHHC14 and DHHC18 to catalyze RAS palmitoylation. These findings provide insights into the regulatory mechanism of RAS palmitoyltransferases.
External linksNat Struct Mol Biol / PubMed:38182928
MethodsEM (single particle)
Resolution3.4 - 3.5 Å
Structure data

34711

8hf3

EMDB-34711, PDB-8hf3:
Cryo-EM structure of human ZDHHC9/GCP16 complex
Method: EM (single particle) / Resolution: 3.4 Å

34717

8hfc

EMDB-34717, PDB-8hfc:
Cryo-EM structure of yeast Erf2/Erf4 complex
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-PLM:
PALMITIC ACID

ChemComp-PX2:
1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE

Source
  • homo sapiens (human)
  • Saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsTRANSFERASE / plamitoytransferase / palmitoylation / DHHC / RAS / palmitoyltransferase / Saccaromyces cerevisiae / RAS2

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