Publication for Cidec and Plin1

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
mmu	Cidec	cell death-inducing DFFA-like effector c	14311			[link]
mmu	Plin1	perilipin 1	103968

Pubmed ID	Priority	Text
27386151	0.99	FSP27 interacts directly with another lipid droplet protein, perilipin 1, which is involved in lipolysis by indirect activation of the adipose triglyceride lipase (ATGL) at the lipid droplet surface.
21103377	0.98	PeriA in white adipocytes reduces lipid droplet size by decreasing FSP27 expression and thereby inducing a brown adipose tissue-like phenotype.
	0.98	Fsp27 was significantly decreased in the WAT of PeriA Tg mice compared with WT mice (WT 1.00+-0.22 vs. Tg 0.18+-0.05, p = 0.0007) (Figure 5A).
	0.98	FSP27 locates on the surface of lipid droplets much like PeriA and functions to promote the formation of unilocular lipid droplet in white adipocytes.
	0.98	PeriA in vivo causes a reduction in FSP27 protein expression.
	0.98	PeriA overexpression causes a significant reduction in FSP27 which is associated with decreased adipocyte size, upregulation of genes involved in fatty acid oxidation and a decrease in lipogenic genes.
	0.98	FSP27 by overexpression of PeriA was the trigger for the down-regulation of RIP140 and up-regulation of PGC1alpha, which caused progenitor adipocytes to differentiate into brown adipocytes rather than white adipocytes.
	0.98	PeriA overexpression results in resistance to diet-induced obesity, increased energy expenditure and reduced lipid synthesis in vivo, and that the basis for these effects was the induction of a a BAT-like phenotype in WAT due to a decrease in FSP27 expression.
	0.97	PeriA in 3T3-L1 adipocytes also reduced FSP27 expression and diminished lipid droplet size.
	0.97	FSP27 protein expression and PeriA expression.
	0.96	PeriA and FSP27 (Figure 6B).
	0.95	FSP27 was directly attenuated by PeriA overexpression in vitro
	0.91	FSP27 is reduced in the WAT of PeriA Tg mice
25695774	0.98	Plin1 and Fsp27 is essential for lipid droplet growth by transferring lipids from small to large droplets.
	0.97	Fsp27 was increased in Plin1-/- adipose tissue (Fig. 2C).
	0.97	Plin1, Plin2 and Fsp27.
	0.97	Fsp27 protein was obviously increased in adipose tissue of Plin1-/- mice.
	0.97	Fsp27 upregulation by Plin1 depletion and vice versa, might be a compensatory action for stabilizing lipid droplets.
	0.97	Plin1-/- SVCs, in which no Plin1 was available to mediate the growth of large lipid droplets, in spite of a compensatory increase in Fsp27.
	0.90	Plin1 and Fsp27, but this phenomenon seems to be neglected except in the report of Sawada et al. Fsp27 mRNA or protein expression is upregulated upon Plin1 knockout or knockdown but downregulated by Plin1 transgene, and vice versa Plin1 mRNA expression is upregulated by FSP27 knockout or knockdown.
	0.68	Fsp27/Cidec) and perilipin 1 (Plin1) lead to partial lipodystrophy.
24040030	0.98	FSP27 has been shown to interact with Plin1 while Plin1 increases the activity of FSP27 in the formation of unilocular LDs in adipocytes.
	0.98	FSP27 and Plin1 interact with each other and are involved in the formation of unilocular lipid droplets.
	0.97	FSP27 and Plin1.
	0.96	Plin1 and Plin2 on lipid droplets, it is possible that FSP27/Plin1 interactions may be primarily involved in the formation of unilocular lipid droplets, while SNAP23/Plin2 interactions may direct the formation of multilocular lipid droplets.
	0.94	Plin1 or FSP27 or with the insulin receptor, GLUT1, or VAMP4.
	0.94	Plin1, GLUT1 (the primary glucose transporter in L cells), FSP27, and VAMP4 were not significantly changed in Plin2 overexpression cells when compared to control cells.
	0.93	FSP27, and Plin1 were not significantly changed in Plin2 overexpression cells when compared to control cells, ruling out effects due to altered expression of these proteins.
18682832	0.98	Fsp27 antibody, we checked the sub-cellular localization of Fsp27 in differentiated 3T3-L1 cells and observed that a fraction of Fsp27 was co-localized with lipid droplet specific marker Perilipin ( Fig. 1D ), consistent with previous observation that overexpression of GFP-Fsp27 fusion protein is targeted to lipid droplet.
	0.96	Fsp27 -/- and Perilipin (Plin) -/- mice have a similar lean phenotype, the molecular mechanism by which Fsp27 and Perilipin control energy storage and lipid droplet formation appears to be different.
	0.55	Fsp27 -/- adipocytes was not due to their defect in differentiation as the levels of adipocyte-specific markers such as Fabp and Perilipin-A were in fact slightly higher in Fsp27 -/- adipocytes (data not shown).
24036367	0.98	CIDE-C interaction with Plin1 on CLDs may facilitate FA flux through CLDs and be crucial to protect the adipose cell against lipotoxicity.
	0.98	Plin1 and CIDE-C and specific over-expression of ATGL in WAT lead to a chronic increase in adipose CLD hydrolysis and a concurrent adaptive response that enhances mitochondrial biogenesis and beta-oxidation, possibly via enhanced production of PPAR ligands.
25125366	0.98	Fsp27) is a lipid droplet-associated protein that promotes lipid droplet (LD) growth and triglyceride (TG) storage in white adipocytes.
	0.98	Plin1 and Plin2 was largely unaffected by the loss of CREBH (Fig., 1A), suggesting that CREBH specifically regulates Fsp27 in the liver.
25418138	0.98	CIDEC; also known in rodents as FSP27 or fat-specific protein 27) is a lipid droplet-associated protein that promotes intracellular triglyceride storage.
	0.98	FSP27 interacts with PLIN1 at the contact sites of nascent LD to facilitate lipid transfer and the formation of unilocular LDs.
25565658	0.98	Fsp27 is a lipid droplet-associated protein almost exclusively expressed in adipocytes where it facilitates unilocular lipid droplet formation.
	0.96	Perilipin1 enhances Fsp27-mediated LD fusion in white adipocytes.
26176546	0.98	Plin1 has been shown to promote lipid droplet growth through an interaction with fat specific protein 27 (Fsp27), a member of the cell death- inducing DFF45 effector (Cide) family of proteins.
	0.96	Plin knockout mice, genetic ablation of Cidea or Cidec results in a lean phenotype, enhanced insulin sensitivity, and resistance to dietary induced obesity.
26639173	0.98	PLIN1 is highly expressed and active, modulating LD enlargement as well as LD lipolysis through interactions with FSP27, HSL and CGI-58.
	0.98	CIDE C (FSP27) was shown to interact with PLIN1 through its CIDE-N domain, leading to increased lipid transfer activity.
21632259	0.98	perilipin 1, Cidec, are associated with increased mitochondrial FA beta-oxidation in adipose cells.
24389130	0.98	Plin family (such as Plin1, or perilipin), the Cide family (such as CIDEC or Fsp27), and several others, with the majority being more highly expressed in BAT than WAT, indicating an important role for lipid droplet access and utilization in brown adipocytes.
24772164	0.98	FSP27/CIDEC, Plin1), has been linked to increased adipocyte lipolysis leading to elevated concentration of circulating FAs, insulin resistance, and ectopic lipid deposition in hepatocytes.
25210844	0.98	CIDEC is a lipid droplet-associated protein expressed in brown adipose tissues which suppresses lipolysis by stimulating the size of lipid droplets and ultimately plays role in the accumulation of triglycerides in adipocytes.
25614121	0.98	Plin1, Plin3, and Cidec, was decreased in shFGF21-infected TG mice (Fig. 6D).
25733711	0.98	Plin1 serves as an Fsp27 activator, increasing Fsp27-mediated lipid exchange, lipid transfer, and droplet growth.
26484280	0.98	Fsp27 is a lipid droplet-associated protein almost exclusively expressed in adipocytes where it facilitates unilocular lipid droplet formation.
27342423	0.98	FSP27/CIDEC, which are involved in LD formation, notably the PAT (perilipin, adipophilin, and the tail-interacting protein of 47 kDa) family proteins, perilipin (PLIN 1-5).
27900258	0.98	Perilipin 1 and Fsp27 are two LD proteins that are critical for lipid storage in adipocytes.
28055005	0.98	Fsp27 is a lipid droplet-associated protein that enhances the formation of enlarged lipids and promotes triglyceride accumulation within lipid droplets, this data shows that Survivin has lipogenic effects.
28874443	0.98	Fsp27, or a combination of ASO-Fsp27 and fenofibrate, resulted in the decrease of multiple lipid droplet-associated (Cidea, Plin1) and lipogenic (Srebp1c, Fasn, Scd1) transcripts.
29454584	0.98	FSP27 promotes the formation of LD-LD fusions on adipocytes and enlarged unilocular LDs in cooperation with perilipin 1, another LD-associated protein.
30871156	0.98	Perilipin1 interacts with FSP27 during lipid droplet fusion at the CIDE-N domain, but not with CIDEA or CIDEB, suggesting that this interaction is specific within white adipose tissue.
31117231	0.98	Cidec-mediated LD fusion, including Plin1, Rab8a, MSS4, and AS160.
31936603	0.98	perilipin1, Fsp27, FAS, and ACC at the RNA level (Figure 2A).
26211746	0.97	Fsp27/Cidec, Plin1) and glucocorticoid metabolism (Hsd11b1) despite normal levels of Ppargamma2.
	0.97	Plin1, Fsp27/Cidec), whereas lipolysis is mediated by lipases (eg, Pnpla2, Lipe) and autophagic processes.
	0.96	Cidec and Plin1 expression in Hdac3 CKO cultures, but had no effect on Ppargamma levels (Fig. 4D).
	0.96	Plin1 and Cidec) were not elevated in osteogenic Hdac3 CKOOsx cultures when dexamethasone was excluded from the culture medium (Fig. 4E).
	0.96	Plin1 and Cidec/Fsp27, in the presence of dexamethasone (Fig. 5G).
	0.95	Plin1 and Fsp27/Cidec were restored (repressed) after adenoviral delivery of V5-Hdac3 (Ad-Hdac3) into Hdac3 CKOOsx cells (Fig. 2C - E).
	0.94	Plin1, Fsp27/Cidec), but relatively little change in Ppargamma2 or fatty acid synthesis (Fasn) and small increases in lipase genes (Pnpla2, Lipe)as compared to control BMSCs (Fig. 2B).
	0.88	Plin1 and Cidec were comparable between control and Hdac3 CKOOsx cultures grown in adipogenic medium (Supporting Fig. 3).
27445983	0.97	Plin1, aP2, FSP27, and Fasn, were increased significantly in HFD groups.
	0.92	Plin1, aP2, Fsp27, and Fasn in exercisers in CTL and HFD groups (Figure 2B).
	0.90	FSP27 and Plin1 were both increased with exercise, in both diet groups (Figure 2D, p < 0.05 for an exercise effect by two-way ANOVA).
24130751	0.97	perilipin 1, perilipin 2/ADRP, and perilipin 3/TIP47) and CIDE family (CIDEA, CIDEB, and CIDEC/FSP27) were first identified in adipose tissue and shown to orchestrate storage and retrieval of triglycerides and mutations in some of these genes result in lipodystrophy and insulin resistance.
	0.95	Fsp27, and Cidea mRNA was reduced by 40%, 75%, and 85%, respectively in the liver of Gcn2 KO mice (Fig. 2A) whereas the expression of Ppargamma1, Plin1, Plin2, and Sgms2 was normal.
26267806	0.97	perilipin 1 interacts with the CIDE-N domain of Fsp27, enhancing lipid exchange, transfer and growth.
	0.88	Fsp27 and perilipin 1 was necessary for efficient droplet growth.
28727234	0.97	Cidec and Plin1.
	0.95	Cidec and Plin1, but did not alter the expression of the adipocyte markers Ppargamma2 and Fasn (Figure 6C).
27884961	0.97	CIDEC (cell death-inducing DFFA-like effector C), also known in mice as Fsp27 (fat-specific protein 27), is a lipid droplet-associated protein that prevents lipid mobilization and promotes intracellular lipid storage.
30482005	0.97	CIDEC, CIDEA and PLIN1, have been demonstrated after the stimulation of browning.
31749714	0.97	Plin1 with a corresponding expression of Cidec at 8 days, facilitated the LDs enlargement in 1CP-treated 3T3-L1 cells, while CIDEA had a central role in packaging newly synthesized triglyceride in LDs for subsequent lipolysis and fatty acid oxidation useful in thermogenic cells.
31959889	0.97	CIDEC was unchanged, PLIN1 protein was significantly decreased during adipocyte differentiation in CTSB-OE cells (Supplementary Fig. 3C,F,G).
23688782	0.96	Plin1 and Fsp27 null mice was the observation that Fsp27 null white adipocytes contained multilocular droplets while they remain unilocular in Plin1 null.
	0.95	Fsp27 loss of function are similar to those observed in Plin1-null mice, including reduced fat mass, increased lipolysis and increased adipocyte beta-oxidation.
	0.55	Plin1 null mice develop insulin resistance by 6 months, but Fsp27 null mice remained insulin sensitive through a 4-month study duration.
28806763	0.96	Plin1, Agpat2, Mogat2, and Cidec (S6 Table).
29264458	0.96	Cidec, and the perilipin Plin2, with lower levels of Cidea and Plin1 .
24133206	0.95	perilipin 1 (Plin1), the major adipocyte protein that coats lipid droplets, and Fsp27, whose mutation results in small and multilocular droplets, similar to the ones seen in lipin 1 knockdown cells.
	0.91	Plin 1 or Fsp27.
	0.56	Plin1 and Fsp27.
28883211	0.95	FSP27 was found to store TAG efficiently in cooperation with several proteins: perilipin 1), adipose triacylglycerol lipase), and Egr1).
30556038	0.95	lipid droplet-associated protein, to bind to lipid droplets as they increase in size, suggesting involvement in the biogenesis of lipid droplets and development of hepatic steatosis.28 Another protein involved in lipid droplet growth is cell death-inducing DNA fragmentation factor-like effector C (cidec); cidec drives lipid transfer from smaller lipid droplets to larger lipid droplets, thus promoting lipid droplet growth.29 We found cidec to be differentially expressed by a fold change of 3.87 in the pFFC-FFC mice when compared to the pChow-FFC mice.
23740690	0.94	perilipin1 or FSP27 leads to increased insulin sensitivity (Martinez-Botas et al,; Nishino et al,; Tansey et al,).
30428424	0.94	CIDEC and perilipin1 knockout mice were protected against obesity and insulin resistance, underscoring the importance of human models in understanding lipid physiology.
31263454	0.94	Plin1 and Cidec were mildly reduced while others were not altered in adipose tissue of adipose-Piezo1-/- mice (Supplementary Figure 6A).
30400205	0.93	FSP27, SREBF1, PLIN4, and SEIPIN and that these proteins could indirectly affect other lipid droplet-related proteins such as PLIN1, PLIN3, PLIN5, FITM1, FITM2, LIPIN1, LIPIN2, etc.
	0.73	PLIN1, PLIN3, and FSP27 increased significantly (p < 0.05), while the expression levels of PLIN5 and SREBP1 decreased significantly (p < 0.05) (Figure 3D).
23967297	0.87	CIDEC and PLIN1 were higher and CXCR1 and SNORD37 were reduced the most in ob/ob mice.
29367353	0.52	Plin1, and Fsp27 were similar between wild-type and Rab3GAP1-deficient cells (Fig. S3 J).