Lysosomal metabolism of lipid-modified proteins

Jui Yun Lu, Sandra L. Hofmann

Research output: Contribution to journalReview article

43 Scopus citations

Abstract

Much is now understood concerning the synthesis of prenylated and palmitoylated proteins, but what is known of their metabolic fate? This review details metabolic pathways for the lysosomal degradation of S-fatty acylated and prenylated proteins. Central to these pathways are two lysosomal enzymes, palmitoyl-protein thioesterase (PPT1) and prenylcysteine lyase (PCL). PPT1 is a soluble lipase that cleaves fatty acids from cysteine residues in proteins during lysosomal protein degradation. Notably, deficiency in the enzyme causes a neurodegenerative lysosomal storage disorder, infantile neuronal ceroid lipofuscinosis. PCL is a membrane-associated flavin-containing lysosomal monooxygenase that metabolizes prenylcysteine to prenyl aldehyde through a completely novel mechanism. The eventual metabolic fates of other lipidated proteins (such as glycosylphosphatidylinositol-anchored and N-myristoylated proteins) are poorly understood, suggesting directions for future research.

Original languageEnglish (US)
Pages (from-to)1352-1357
Number of pages6
JournalJournal of lipid research
Volume47
Issue number7
DOIs
StatePublished - 2006

Keywords

  • Lysosomal enzymes
  • Monooxygenases
  • Posttranslational lipid modifications
  • Prenylation
  • S-palmitoylation
  • Thioesterases

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Cell Biology

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