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词条 Perilipin-4
释义

  1. Structure

      Gene    Protein  

  2. Function

  3. Clinical significance

  4. Interactions

  5. References

  6. Further reading

{{Infobox_gene}}Perilipin 4, also known as S3-12, is a protein that in humans is encoded by the PLIN4 gene on chromosome 19.[1][2] It is highly expressed in white adipose tissue, with lower expression in heart, skeletal muscle, and brown adipose tissue.[3] PLIN4 coats lipid droplets in adipocytes to protect them from lipases.[4][5] The PLIN4 gene may be associated with insulin resistance and obesity risk.[6]

Structure

Gene

The PLIN4 gene resides on chromosome 19 at the band 19p13.3 and contains 9 exons.[1]

Protein

This protein belongs to the perilipin family and contains 27 33-amino acid approximate tandem repeats.[4] It is also one of the perilipin members of the PATS (PLIN, ADFP, TIP47, S3-12) family, which is named after structural proteins that share high amino acid sequence similarity and associate with lipid droplets.[2] It shares a conserved C-terminal of 14 amino acid residues that folds into a hydrophobic cleft with other PATS members; however, it is missing the conserved N-terminal region of approximately 100 amino acid residues. Within the sequence of 33-amino acid repeats, PLIN4 contains a long stretch of imperfect 11-mer repeats predicted to form amphipathic helices with three helical turns per 11 amino acid residues. This 11-mer repeats tract is proposed to anchor the protein to the phospholipid monolayer of lipid droplets for its assembly, though no targeting sequence has yet been found in PLIN4.[3]

Function

PLIN4 is a member of the perilipin family, a group of proteins that coat lipid droplets in adipocytes,[5] the adipose tissue cells that are responsible for storing fat. Perilipin acts as a protective coating from the body’s natural lipases, such as hormone-sensitive lipase,[6] which break triglycerides into glycerol and free fatty acids for use in metabolism, a process called lipolysis.[7] In humans, perilipin is expressed as 5 different isoforms; it is currently understood that the level of expression for each isoform is dependent on factors such as sex, body mass index, and level of endurance exercise.[8]

PLIN4 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.

Clinical significance

The proteins in the Perilipin family are crucial regulators of lipid storage.[7] PLIN4 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.[9] Perilipin-null mice also exhibit enhanced leptin production and a greater tendency to develop insulin resistance than wild-type mice.

The PLIN4 gene, along with PLIN2, PLIN3, and PLIN5, have been associated with variance in body-weight regulation and may be a genetic influence on obesity risk in humans.[10]

Interactions

PLIN4 has been shown to interact with Caspase 8 and Ubiquitin C.[11]

References

1. ^1 {{cite web | title = Entrez Gene: Perilipin 4 | url = https://www.ncbi.nlm.nih.gov/gene/729359 }}
2. ^1 {{cite journal | vauthors = Cusano NE, Kiel DP, Demissie S, Karasik D, Adrienne Cupples L, Corella D, Gao Q, Richardson K, Yiannakouris N, Ordovas JM | title = A Polymorphism in a gene encoding Perilipin 4 is associated with height but not with bone measures in individuals from the Framingham Osteoporosis Study | journal = Calcified Tissue International | volume = 90 | issue = 2 | pages = 96–107 | date = February 2012 | pmc = 3628693 | doi = 10.1007/s00223-011-9552-7 | pmid = 22210160 }}
3. ^1 {{cite journal | vauthors = Brasaemle DL | title = Thematic review series: adipocyte biology. The perilipin family of structural lipid droplet proteins: stabilization of lipid droplets and control of lipolysis | journal = Journal of Lipid Research | volume = 48 | issue = 12 | pages = 2547–59 | date = December 2007 | doi = 10.1194/jlr.R700014-JLR200 | pmid = 17878492 }}
4. ^{{UniProt Full|Q96Q06|PLIN4 - Perilipin-4 - Homo sapiens - PLIN4 gene & protein}}
5. ^1 {{cite journal | vauthors = Greenberg AS, Egan JJ, Wek SA, Garty NB, Blanchette-Mackie EJ, Londos C | title = Perilipin, a major hormonally regulated adipocyte-specific phosphoprotein associated with the periphery of lipid storage droplets | journal = The Journal of Biological Chemistry | volume = 266 | issue = 17 | pages = 11341–6 | date = June 1991 | pmid = 2040638 | doi = }}
6. ^1 {{cite web | url = http://www.scientificamerican.com/article.cfm?id=making-fat-proof-mice | title = Making Fat-proof Mice | author = Wong K | authorlink = | date = 2000-11-29 | format = | website = | publisher = Scientific American | pages = | archiveurl = | archivedate = | quote = | accessdate = 2009-05-22}}
7. ^1 {{cite journal | vauthors = Wolins NE, Skinner JR, Schoenfish MJ, Tzekov A, Bensch KG, Bickel PE | title = Adipocyte protein S3-12 coats nascent lipid droplets | journal = The Journal of Biological Chemistry | volume = 278 | issue = 39 | pages = 37713–21 | date = September 2003 | pmid = 12840023 | doi = 10.1074/jbc.M304025200 }}
8. ^{{cite journal | vauthors = Peters SJ, Samjoo IA, Devries MC, Stevic I, Robertshaw HA, Tarnopolsky MA | title = Perilipin family (PLIN) proteins in human skeletal muscle: the effect of sex, obesity, and endurance training | journal = Applied Physiology, Nutrition, and Metabolism = Physiologie Appliquee, Nutrition et Metabolisme | volume = 37 | issue = 4 | pages = 724–35 | date = August 2012 | pmid = 22667335 | doi = 10.1139/h2012-059 }}
9. ^telegraph.co.uk, 19 June 2001, {{cite news |url=https://www.telegraph.co.uk/news/worldnews/1376193/Couch-potato-mice-discover-the-lazy-way-to-stay-slim.html |title=Couch potato mice discover the lazy way to stay slim |work= The Daily Telegraph|accessdate=2008-09-03 | location=London | first=Roger | last=Highfield | date=2000-11-29}}
10. ^1 {{cite journal | vauthors = Soenen S, Mariman EC, Vogels N, Bouwman FG, den Hoed M, Brown L, Westerterp-Plantenga MS | title = Relationship between perilipin gene polymorphisms and body weight and body composition during weight loss and weight maintenance | journal = Physiology & Behavior | volume = 96 | issue = 4–5 | pages = 723–8 | date = March 2009 | pmid = 19385027 | doi = 10.1016/j.physbeh.2009.01.011 }}
11. ^{{cite web | title = PLIN4 Results Summary | url = http://thebiogrid.org/609760|website=BioGrid | publisher = Tyerslab.com | accessdate = 18 May 2015}}

Further reading

{{refbegin|33em}}
  • {{cite journal | vauthors = Richardson K, Louie-Gao Q, Arnett DK, Parnell LD, Lai CQ, Davalos A, Fox CS, Demissie S, Cupples LA, Fernandez-Hernando C, Ordovas JM | title = The PLIN4 variant rs8887 modulates obesity related phenotypes in humans through creation of a novel miR-522 seed site | journal = PLoS One | volume = 6 | issue = 4 | pages = e17944 | date = April 2011 | pmid = 21533135 | pmc = 3080366 | doi = 10.1371/journal.pone.0017944 }}
  • {{cite journal | vauthors = Sone Y, Yamaguchi K, Fujiwara A, Kido T, Kawahara K, Ishiwaki A, Kondo K, Morita Y, Tominaga N, Otsuka Y | title = Association of lifestyle factors, polymorphisms in adiponectin, perilipin and hormone sensitive lipase, and clinical markers in Japanese males | journal = Journal of Nutritional Science and Vitaminology | volume = 56 | issue = 2 | pages = 123–31 | year = 2010 | pmid = 20495294 | doi = 10.3177/jnsv.56.123 }}
  • {{cite journal | vauthors = Kimmel AR, Brasaemle DL, McAndrews-Hill M, Sztalryd C, Londos C | title = Adoption of PERILIPIN as a unifying nomenclature for the mammalian PAT-family of intracellular lipid storage droplet proteins | journal = Journal of Lipid Research | volume = 51 | issue = 3 | pages = 468–71 | date = March 2010 | pmid = 19638644 | pmc = 2817576 | doi = 10.1194/jlr.R000034 }}
  • {{cite journal | vauthors = Wolins NE, Skinner JR, Schoenfish MJ, Tzekov A, Bensch KG, Bickel PE | title = Adipocyte protein S3-12 coats nascent lipid droplets | journal = The Journal of Biological Chemistry | volume = 278 | issue = 39 | pages = 37713–21 | date = September 2003 | pmid = 12840023 | doi = 10.1074/jbc.M304025200 }}
  • {{cite journal | vauthors = Nagase T, Kikuno R, Ohara O | title = Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins | journal = DNA Research | volume = 8 | issue = 4 | pages = 179–87 | date = August 2001 | pmid = 11572484 | doi = 10.1093/dnares/8.4.179 }}
  • {{cite journal | vauthors = Cusano NE, Kiel DP, Demissie S, Karasik D, Adrienne Cupples L, Corella D, Gao Q, Richardson K, Yiannakouris N, Ordovas JM | title = A Polymorphism in a gene encoding Perilipin 4 is associated with height but not with bone measures in individuals from the Framingham Osteoporosis Study | journal = Calcified Tissue International | volume = 90 | issue = 2 | pages = 96–107 | date = February 2012 | pmid = 22210160 | pmc = 3628693 | doi = 10.1007/s00223-011-9552-7 }}
  • {{cite journal | vauthors = Peters SJ, Samjoo IA, Devries MC, Stevic I, Robertshaw HA, Tarnopolsky MA | title = Perilipin family (PLIN) proteins in human skeletal muscle: the effect of sex, obesity, and endurance training | journal = Applied Physiology, Nutrition, and Metabolism = Physiologie Appliquee, Nutrition et Metabolisme | volume = 37 | issue = 4 | pages = 724–35 | date = August 2012 | pmid = 22667335 | doi = 10.1139/h2012-059 }}
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