Modification of N-glycosylation modulates the secretion and lipolytic function of apoptosis inhibitor of macrophage (AIM)

Mayumi Mori, Hiroki Kimura, Yoshihiro Iwamura, Satoko Arai, Toru Miyazaki

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

Abstract

The mouse macrophage-derived apoptosis inhibitor of macrophage (AIM), which is incorporated into adipocytes and induces lipolysis by suppressing fatty acid synthase (FAS) activity, possesses three potential N-glycosylation sites. Inactivation of N-glycosylation sites revealed that mouse AIM contains two N-glycans in the first and second scavenger receptor cysteine-rich domains, and that depletion of N-glycans decreased AIM secretion from producing cells. Interestingly, the lack of N-glycans increased AIM lipolytic activity through enhancing AIM incorporation into adipocytes. Although human AIM contains no N-glycan, attachment of N-glycans increased AIM secretion. Thus, the N-glycosylation plays important roles in the secretion and lipolytic function of AIM. Structured summary of protein interactions: AIM physically interacts with FAS by anti tag coimmunoprecipitation (View interaction).

Original languageEnglish (US)
Pages (from-to)3569-3574
Number of pages6
JournalFEBS Letters
Volume586
Issue number20
DOIs
StatePublished - Oct 19 2012
Externally publishedYes

Keywords

  • Apoptosis inhibitor of macrophage (AIM)
  • CD36
  • Fatty acid synthase (FAS)
  • Lipid droplet coating protein
  • Lipolysis
  • N-Glycan

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint

Dive into the research topics of 'Modification of N-glycosylation modulates the secretion and lipolytic function of apoptosis inhibitor of macrophage (AIM)'. Together they form a unique fingerprint.

Cite this