The lipid droplet coat protein perilipin 5 also localizes to muscle mitochondria

@article{Bosma2011TheLD,
  title={The lipid droplet coat protein perilipin 5 also localizes to muscle mitochondria},
  author={M. Bosma and R. Minnaard and L. Sparks and G. Schaart and M. Losen and M. D. de Baets and H. Duimel and S. Kersten and P. Bickel and P. Schrauwen and M. Hesselink},
  journal={Histochemistry and Cell Biology},
  year={2011},
  volume={137},
  pages={205 - 216}
}
Perilipin 5 (PLIN5/OXPAT) is a lipid droplet (LD) coat protein mainly present in tissues with a high fat-oxidative capacity, suggesting a role for PLIN5 in facilitating fatty acid oxidation. Here, we investigated the role of PLIN5 in fat oxidation in skeletal muscle. In human skeletal muscle, we observed that PLIN5 (but not PLIN2) protein content correlated tightly with OXPHOS content and in rat muscle PLIN5 content correlated with mitochondrial respiration rates on a lipid-derived substrate… Expand
Perilipin 5, a lipid droplet protein adapted to mitochondrial energy utilization
TLDR
In-vivo and in-vitro data suggest that Plin5 is part of a cell-adaptive response to high lipid oxidative metabolism to protect lipid droplet storage against neutral lipases and, so, limit fatty acid accumulation. Expand
Fatty acids regulate perilipin5 in muscle by activating PPARδ[S]
TLDR
This study reveals that muscle cells respond to elevated FAs by increasing transcription of several perilipin LD-coating proteins, which renders the muscle better equipped to sequester incoming FAs into cytosolic LDs. Expand
Piecing together the puzzle of perilipin proteins and skeletal muscle lipolysis.
  • R. MacPherson, S. J. Peters
  • Biology, Medicine
  • Applied physiology, nutrition, and metabolism = Physiologie appliquee, nutrition et metabolisme
  • 2015
TLDR
Results from work in these models support a role for PLIN proteins in sequestering lipases during basal conditions and in potentially working together for lipase translocation and activity during lipolysis. Expand
Mitochondria Bound to Lipid Droplets Have Unique Bioenergetics, Composition, and Dynamics that Support Lipid Droplet Expansion.
TLDR
It is concluded that PDM represent a segregated mitochondrial population with unique structure and function that supports triacylglyceride synthesis. Expand
Higher PLIN5 but not PLIN3 content in isolated skeletal muscle mitochondria following acute in vivo contraction in rat hindlimb
TLDR
PLIN3 and PLIN5 may be working together on the lipid droplet and mitochondria during contraction‐induced lipolysis, which is consistent with a role in facilitating/regulating mitochondrial fatty acid oxidation. Expand
Overexpression of PLIN5 in skeletal muscle promotes oxidative gene expression and intramyocellular lipid content without compromising insulin sensitivity.
TLDR
In contrast to the effects of PLIN2 overexpression, microarray data analysis revealed a gene expression profile favoring FA oxidation and improved mitochondrial function that promoted expression of a cluster of genes under control of PPARα and PGC1α involved in FA catabolism and mitochondrial oxidation. Expand
Adipocyte lipolysis affects Perilipin 5 and cristae organization at the cardiac lipid droplet-mitochondrial interface
TLDR
The results support the concept that the interface between LD and cardiac mitochondria represents an organized and dynamic “metabolic synapse” that is highly responsive to FA trafficking. Expand
VITAMIN D WORKS THROUGH THE LIPID DROPLET PROTEIN PLIN2 TO AUGMENT MITOCHONDRIAL FUNCTION IN SKELETAL MUSCLE
OF DISSERTATION VITAMIN D WORKS THROUGH THE LIPID DROPLET PROTEIN PLIN2 TO AUGMENT MITOCHONDRIAL FUNCTION IN SKELETAL MUSCLE Vitamin D has been connected with increased intramyocellular lipid (IMCL)Expand
Skeletal Muscle Perilipin 3 and Coatomer Proteins Are Increased following Exercise and Are Associated with Fat Oxidation
TLDR
The effects of lipolytic stimulation in vitro in primary human myotubes as well as in vivo following an acute exercise bout are explored to provide novel observational insight into the possible relationships between lipolysis and PLIN3 along with these coatomoer GTPase proteins in human skeletal muscle. Expand
The Interplay of Protein Kinase A and Perilipin 5 Regulates Cardiac Lipolysis*♦
TLDR
It is shown that the lipolytic barrier of Plin5-enriched LDs, either prepared from cardiac tissue of CM-Plin5 mice or PlIn5-transfected cells, is abrogated by incubation with PKA, revealing a critical role for PKA in Plin 5-regulated lipolysis. Expand
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References

SHOWING 1-10 OF 46 REFERENCES
Perilipin 5, a lipid droplet-associated protein, provides physical and metabolic linkage to mitochondria[S]
TLDR
Results suggest that Plin5 regulates oxidative LD hydrolysis and controls local FA flux to protect mitochondria against excessive exposure to FA during physiological stress. Expand
OXPAT/PAT-1 Is a PPAR-Induced Lipid Droplet Protein That Promotes Fatty Acid Utilization
TLDR
The collective data in cells, mice, and humans suggest that OXPAT is a marker for PPAR activation and fatty acid oxidation, which likely contributes to adaptive responses to the fatty acid burden that accompanies fasting, insulin deficiency, and overnutrition, responses that are defective in obesity and type 2 diabetes. Expand
Overexpression of carnitine palmitoyltransferase I in skeletal muscle in vivo increases fatty acid oxidation and reduces triacylglycerol esterification.
TLDR
It is demonstrated that acute overexpression of CPT I in muscle leads to a repartitioning of FAs away from esterification and toward oxidation and highlight the importance of C PT I in regulating muscle FA metabolism. Expand
Interactions of Perilipin-5 (Plin5) with Adipose Triglyceride Lipase*
TLDR
Analysis of chimeric and mutant perilipin proteins demonstrated that amino acids 200–463 are necessary and sufficient to bind both Atgl and Abhd5 and that the C-terminal 64 amino acids of Plin5 are critical for the differential binding of Atgl to Plin 5 and Plin1. Expand
Proteomic Analysis of Proteins Associated with Lipid Droplets of Basal and Lipolytically Stimulated 3T3-L1 Adipocytes*
TLDR
Adipocytes contain specific structural proteins as well as lipid metabolic enzymes; the structural reorganization of lipid droplets in response to the hormonal stimulation of lipolysis is accompanied by increases in the relative mass of several proteins and the recruitment of additional proteins. Expand
PAT proteins, an ancient family of lipid droplet proteins that regulate cellular lipid stores.
TLDR
How the PAT proteins regulate cellular lipid metabolism both in mammals and in model organisms is discussed. Expand
Perilipin is located on the surface layer of intracellular lipid droplets in adipocytes.
TLDR
Perilipin's singular location on the surface monolayer of intracellular lipid droplets supports an intimate role for the protein in the triacylglycerol metabolic functions of adipocytes, and studies in mammary gland show that perilipin immunostaining will be a valuable tool for the identification of tissue adipocytes severely depleted of their triacy lysergic stores and thus without their characteristic spherical shape. Expand
Role of caveolin-1 in the modulation of lipolysis and lipid droplet formation.
TLDR
The data provide the first molecular genetic evidence that caveolin-1 plays a critical functional and structural role in the modulation of both lipid droplet biogenesis and metabolism in vivo. Expand
MLDP, a Novel PAT Family Protein Localized to Lipid Droplets and Enriched in the Heart, Is Regulated by Peroxisome Proliferator-activated Receptor α*
TLDR
Results indicate that MLDP is a bona fide new PAT family member localized in LDs, and its expression depends on the physiological conditions and the action of PPARα. Expand
Adipocyte differentiation-related protein and OXPAT in rat and human skeletal muscle: involvement in lipid accumulation and type 2 diabetes mellitus.
TLDR
Investigation of the role of PAT proteins OXPAT and ADRP in skeletal muscle lipid metabolism and their putative role in modulating insulin sensitivity indicates involvement in muscular lipid accumulation and type 2 diabetes. Expand
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