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Palmitoylation Code and Endosomal Sorting Regulate ABHD17A Plasma Membrane Targeting and Activity.

Byeol-I Kim1, Jun-Hee Yeon1, Byung-Chang Suh1

  • 1Department of Brain Sciences, Daegu Gyeongbuk Institute of Science and Technology (DGIST), Daegu 42988, Republic of Korea.

International Journal of Molecular Sciences
|October 29, 2025
PubMed
Summary
This summary is machine-generated.

Protein S-palmitoylation is a reversible lipid modification. This study reveals a palmitoylation code in ABHD17A that controls its plasma membrane targeting and depalmitoylase activity, essential for protein function.

Keywords:
ABHD17depalmitoylaselipid modificationpalmitoylation

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Protein S-palmitoylation is a reversible lipid modification regulating protein function.
  • The depalmitoylase ABHD17A's cellular localization and the role of its own palmitoylation are unclear.

Purpose of the Study:

  • To elucidate the role of ABHD17A palmitoylation in its function.
  • To identify the specific palmitoylation sites and their impact on ABHD17A localization and activity.

Main Methods:

  • Site-directed mutagenesis of ABHD17A cysteine residues.
  • Analysis of protein localization using microscopy.
  • Biochemical assays to assess depalmitoylase activity.
  • Sequence analysis and comparative studies of ABHD17 family members.

Main Results:

  • A palmitoylation code in the N-terminal cysteine cluster of ABHD17A governs its plasma membrane targeting.
  • N-terminal palmitoylation is crucial for plasma membrane localization.
  • Modifications in the middle region (C14, C15) are critical for plasma membrane targeting and catalytic activity.
  • Specific tyrosine-based motifs (YXXØ) are required for endosomal sorting and surface abundance.
  • Acylation states are influenced by the palmitoylation code, with conserved requirements in ABHD17B and ABHD17C.

Conclusions:

  • ABHD17A utilizes a stepwise delivery mechanism to reach the plasma membrane.
  • Palmitoylation code dictates ABHD17A's subcellular distribution and activity on membrane-bound substrates.
  • Understanding ABHD17A palmitoylation provides insights into regulation of depalmitoylase function.