RGD Reference Report - Perilipin 5, a lipid droplet-associated protein, provides physical and metabolic linkage to mitochondria. - Rat Genome Database

Send us a Message



Submit Data |  Help |  Video Tutorials |  News |  Publications |  Download |  REST API |  Citing RGD |  Contact   

Perilipin 5, a lipid droplet-associated protein, provides physical and metabolic linkage to mitochondria.

Authors: Wang, H  Sreenivasan, U  Hu, H  Saladino, A  Polster, BM  Lund, LM  Gong, DW  Stanley, WC  Sztalryd, C 
Citation: Wang H, etal., J Lipid Res. 2011 Dec;52(12):2159-68. doi: 10.1194/jlr.M017939. Epub 2011 Aug 31.
RGD ID: 8553283
Pubmed: PMID:21885430   (View Abstract at PubMed)
PMCID: PMC3220284   (View Article at PubMed Central)
DOI: DOI:10.1194/jlr.M017939   (Journal Full-text)

Maintaining cellular lipid homeostasis is crucial to oxidative tissues, and it becomes compromised in obesity. Lipid droplets (LD) play a central role in lipid homeostasis by mediating fatty acid (FA) storage in the form of triglyceride, thereby lowering intracellular levels of lipids that mediate cellular lipotoxicity. LDs and mitochondria have interconnected functions, and anecdotal evidence suggests they physically interact. However, the mechanisms of interaction have not been identified. Perilipins are LD-scaffolding proteins and potential candidates to play a role in their interaction with mitochondria. We examined the contribution of LD perilipin composition to the physical and metabolic interactions between LD and mitochondria using multiple techniques: confocal imaging, electron microscopy (EM), and lipid storage and utilization measurements. Using neonatal cardiomyocytes, reconstituted cell culture models, and rodent heart tissues, we found that perilipin 5 (Plin5) recruits mitochondria to the LD surface through a C-terminal region. Compared with control cells, Plin5-expressing cells show decreased LD hydrolysis, decreased palmitate beta-oxidation, and increased palmitate incorporation into triglycerides in basal conditions, whereas in stimulated conditions, LD hydrolysis inhibition is lifted and FA released for beta-oxidation. These results suggest that Plin5 regulates oxidative LD hydrolysis and controls local FA flux to protect mitochondria against excessive exposure to FA during physiological stress.



Gene Ontology Annotations    Click to see Annotation Detail View

Cellular Component
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Plin5Ratlipid droplet located_inIDA PMID:21885430UniProt 
Plin5Ratmitochondrion NOT|located_inIDA PMID:21885430UniProt 

Objects Annotated

Genes (Rattus norvegicus)
Plin5  (perilipin 5)


Additional Information