Research

Hormonal

Phosphorylation of Perilipin at specific sites (Ser-492 and Ser-517) by PKA is required to release Abhd5, allowing it to interact with and activate Atgl, thereby stimulating lipolysis.

This research identifies the specific molecular 'switch' (PKA phosphorylation of Perilipin) that turns on fat burning. When hormones signal the body to use energy, this switch releases the enzyme (Abhd5) that activates fat breakdown. This underscores the importance of hormonal triggers (like exercise or fasting) in mobilizing stored fat.

GoodSupportsHIGH confidence
Phosphorylation of Plin on serine 492 or serine 517 rapidly releases Abhd5 from Plin, allowing Abhd5 to directly interact with Atgl.
James G. Granneman et al. · Journal of Biological Chemistry · 2009

Why this rating

Strong evidence from mutation studies and FRET/BiFC assays showing site-specific requirements.

Source

Perilipin Controls Lipolysis by Regulating the Interactions of AB-hydrolase Containing 5 (Abhd5) and Adipose Triglyceride Lipase (Atgl)

James G. Granneman et al. · Journal of Biological Chemistry · 2009

DOI 10.1074/jbc.m109.068478

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DOI resolved against Crossref · corpus check 2026-06-10

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