Summary: Perilipin family
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Perilipin Edit Wikipedia article
|External IDs||ChEMBL: GeneCards:|
|RNA expression pattern|
Perilipin, also known as lipid droplet-associated protein or PLIN, is a protein that, in humans, is encoded by the PLIN gene. The perilipins are a family of proteins that associate with the surface of lipid droplets. Phosphorylation of perilipin is essential for the mobilization of fats in adipose tissue.
Perilipin is a protein that coats lipid droplets in adipocytes, the fat-storing cells in adipose tissue. Perilipin acts as a protective coating from the body’s natural lipases, such as hormone-sensitive lipase, which break triglycerides into glycerol and free fatty acids for use in metabolism, a process called lipolysis. In humans, perilipin is expressed in three different isoforms, A, B, and C, and perilipin A is the most abundant protein associated with the adipocyte lipid droplets.
Perilipin is hyperphosphorylated by PKA following β-adrenergic receptor activation. Phosphorylated perilipin changes conformation, exposing the stored lipids to hormone-sensitive lipase-mediated lipolysis. Although PKA also phosphorylates hormone-sensitive lipase, which can increase its activity, the more than 50-fold increase in fat mobilization (triggered by epinephrine) is primarily due to perilipin phosphorylation.
Perilipin is an important regulator of lipid storage. Perilipin expression is elevated in obese animals and humans. Perilipin-null mice eat more food than wild-type mice, but gain 1/3 less fat than wild-type mice on the same diet; perilipin-null mice are thinner, with more lean muscle mass. Perilipin-null mice also exhibit enhanced leptin production and a greater tendency to develop insulin resistance than wild-type mice.
Polymorphisms in the human perilipin (PLIN) gene have been associated with variance in body-weight regulation and may be a genetic influence on obesity risk in humans. In particular, variants 13041A>G and 14995A>T have been associated with increased risk of obesity in women and 11482G>A has been associated with decreased perilipin expression and increased lipolysis in women.
Perilipin family of proteins
Perilipin is part of a gene family with five currently-known members. In vertebrates, closely related genes include adipophilin (also known as adipose differentiation-related protein), TIP47, and LSDP5 (also called MLDP and OXPAT). Insects express related proteins, LSD1 and LSD2, in fat bodies.
- "Entrez Gene: PLIN perilipin".
- Mobilization and Cellular Uptake of Stored Fats (with Animation)
- Greenberg AS, Egan JJ, Wek SA, Garty NB, Blanchette-Mackie EJ, Londos C (June 1991). "Perilipin, a major hormonally regulated adipocyte-specific phosphoprotein associated with the periphery of lipid storage droplets". J. Biol. Chem. 266 (17): 11341–6. PMID 2040638.
- Wong K (2000-11-29). "Making Fat-proof Mice". Scientific American. Retrieved 2009-05-22.
- Brasaemle DL, Subramanian V, Garcia A, Marcinkiewicz A, Rothenberg A (June 2009). "Perilipin A and the control of triacylglycerol metabolism". Mol. Cell. Biochem. 326 (1-2): 15–21. doi:10.1007/s11010-008-9998-8. PMID 19116774.
- telegraph.co.uk, 19 June 2001, Highfield, Roger (2000-11-29). "Couch potato mice discover the lazy way to stay slim". The Daily Telegraph (London). Retrieved 2008-09-03.
- Soenen S, Mariman EC, Vogels N, Bouwman FG, den Hoed M, Brown L, Westerterp-Plantenga MS (March 2009). "Relationship between perilipin gene polymorphisms and body weight and body composition during weight loss and weight maintenance". Physiol. Behav. 96 (4-5): 723–8. doi:10.1016/j.physbeh.2009.01.011. PMID 19385027.
- Qi L, Shen H, Larson I, Schaefer EJ, Greenberg AS, Tregouet DA, Corella D, Ordovas JM (November 2004). "Gender-specific association of a perilipin gene haplotype with obesity risk in a white population". Obes. Res. 12 (11): 1758–65. doi:10.1038/oby.2004.218. PMID 15601970.
- Corella D, Qi L, Sorlí JV, Godoy D, Portolés O, Coltell O, Greenberg AS, Ordovas JM (September 2005). "Obese subjects carrying the 11482G>A polymorphism at the perilipin locus are resistant to weight loss after dietary energy restriction". J. Clin. Endocrinol. Metab. 90 (9): 5121–6. doi:10.1210/jc.2005-0576. PMID 15985482.
- Brasaemle DL (December 2007). "Thematic review series: adipocyte biology. The perilipin family of structural lipid droplet proteins: stabilization of lipid droplets and control of lipolysis". J. Lipid Res. 48 (12): 2547–59. doi:10.1194/jlr.R700014-JLR200. PMID 17878492.
- Tai ES, Ordovas JM (2007). "The role of perilipin in human obesity and insulin resistance.". Curr. Opin. Lipidol. 18 (2): 152–6. doi:10.1097/MOL.0b013e328086aeab. PMID 17353663.
- Nishiu J, Tanaka T, Nakamura Y (1998). "Isolation and chromosomal mapping of the human homolog of perilipin (PLIN), a rat adipose tissue-specific gene, by differential display method.". Genomics 48 (2): 254–7. doi:10.1006/geno.1997.5179. PMID 9521880.
- Souza SC, Muliro KV, Liscum L, et al. (2002). "Modulation of hormone-sensitive lipase and protein kinase A-mediated lipolysis by perilipin A in an adenoviral reconstituted system.". J. Biol. Chem. 277 (10): 8267–72. doi:10.1074/jbc.M108329200. PMID 11751901.
- Hagström-Toft E, Qvisth V, Nennesmo I, et al. (2002). "Marked heterogeneity of human skeletal muscle lipolysis at rest.". Diabetes 51 (12): 3376–83. doi:10.2337/diabetes.51.12.3376. PMID 12453889.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Mottagui-Tabar S, Rydén M, Löfgren P, et al. (2004). "Evidence for an important role of perilipin in the regulation of human adipocyte lipolysis.". Diabetologia 46 (6): 789–97. doi:10.1007/s00125-003-1112-x. PMID 12802495.
- Wang Y, Sullivan S, Trujillo M, et al. (2004). "Perilipin expression in human adipose tissues: effects of severe obesity, gender, and depot.". Obes. Res. 11 (8): 930–6. doi:10.1038/oby.2003.128. PMID 12917496.
- Zhang HH, Souza SC, Muliro KV, et al. (2004). "Lipase-selective functional domains of perilipin A differentially regulate constitutive and protein kinase A-stimulated lipolysis.". J. Biol. Chem. 278 (51): 51535–42. doi:10.1074/jbc.M309591200. PMID 14527948.
- Kern PA, Di Gregorio G, Lu T, et al. (2004). "Perilipin expression in human adipose tissue is elevated with obesity.". J. Clin. Endocrinol. Metab. 89 (3): 1352–8. doi:10.1210/jc.2003-031388. PMID 15001633.
- Arvidsson E, Blomqvist L, Rydén M (2004). "Depot-specific differences in perilipin mRNA but not protein expression in obesity.". J. Intern. Med. 255 (5): 595–601. doi:10.1111/j.1365-2796.2004.01314.x. PMID 15078502.
- Dalen KT, Schoonjans K, Ulven SM, et al. (2004). "Adipose tissue expression of the lipid droplet-associating proteins S3-12 and perilipin is controlled by peroxisome proliferator-activated receptor-gamma.". Diabetes 53 (5): 1243–52. doi:10.2337/diabetes.53.5.1243. PMID 15111493.
- Qi L, Corella D, Sorlí JV, et al. (2005). "Genetic variation at the perilipin (PLIN) locus is associated with obesity-related phenotypes in White women.". Clin. Genet. 66 (4): 299–310. doi:10.1111/j.1399-0004.2004.00309.x. PMID 15355432.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Yan W, Chen S, Huang J, et al. (2005). "Polymorphisms in PLIN and hypertension combined with obesity and lipid profiles in Han Chinese.". Obes. Res. 12 (11): 1733–7. doi:10.1038/oby.2004.214. PMID 15601966.
- Qi L, Shen H, Larson I, et al. (2005). "Gender-specific association of a perilipin gene haplotype with obesity risk in a white population.". Obes. Res. 12 (11): 1758–65. doi:10.1038/oby.2004.218. PMID 15601970.
- Qi L, Tai ES, Tan CE, et al. (2005). "Intragenic linkage disequilibrium structure of the human perilipin gene (PLIN) and haplotype association with increased obesity risk in a multiethnic Asian population.". J. Mol. Med. 83 (6): 448–56. doi:10.1007/s00109-004-0630-4. PMID 15770500.
- Forcheron F, Legedz L, Chinetti G, et al. (2005). "Genes of cholesterol metabolism in human atheroma: overexpression of perilipin and genes promoting cholesterol storage and repression of ABCA1 expression.". Arterioscler. Thromb. Vasc. Biol. 25 (8): 1711–7. doi:10.1161/01.ATV.0000174123.19103.52. PMID 15961705.
- Corella D, Qi L, Sorlí JV, et al. (2005). "Obese subjects carrying the 11482G>A polymorphism at the perilipin locus are resistant to weight loss after dietary energy restriction.". J. Clin. Endocrinol. Metab. 90 (9): 5121–6. doi:10.1210/jc.2005-0576. PMID 15985482.
- Moore HP, Silver RB, Mottillo EP, et al. (2006). "Perilipin targets a novel pool of lipid droplets for lipolytic attack by hormone-sensitive lipase.". J. Biol. Chem. 280 (52): 43109–20. doi:10.1074/jbc.M506336200. PMID 16243839.
- Shimizu M, Akter MH, Emi Y, et al. (2007). "Peroxisome proliferator-activated receptor subtypes differentially cooperate with other transcription factors in selective transactivation of the perilipin/PEX11 alpha gene pair.". J. Biochem. 139 (3): 563–73. doi:10.1093/jb/mvj053. PMID 16567422.
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Perilipin family Provide feedback
The perilipin family includes lipid droplet-associated protein (perilipin) and adipose differentiation-related protein (adipophilin).
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR004279The perilipin family includes lipid droplet-associated protein (perilipin) and adipose differentiation-related protein (adipophilin). Perilipin is a modulator of adipocyte lipid metabolism and adipophilinis involved in the development and maintenance of adipose tissue. Other proteins belong to this group include TIP47, a cargo selection device for mannose 6-phosphate receptor trafficking [PUBMED:9590177].
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Key: available, not generated, — not available.
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|Seed source:||Pfam-B_1154 (release 6.4)|
|Number in seed:||17|
|Number in full:||474|
|Average length of the domain:||278.60 aa|
|Average identity of full alignment:||26 %|
|Average coverage of the sequence by the domain:||73.43 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
|Download:||download the raw HMM for this family|
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Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
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The tree shows the occurrence of this domain across different species. More...
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For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
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We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Perilipin domain has been found. There are 1 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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