4mac

From Proteopedia

(Difference between revisions)

Revision as of 11:05, 21 December 2022

Crystal structure of CIDE-N domain of FSP27

Structural highlights

4mac is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CIDEC_MOUSE Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair. Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1. May act as a CEBPB coactivator in the white adipose tissue to control the expression of a subset of CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment. As mature adipocytes, that express high CIDEC levels, are quite resistant to apoptotic stimuli, the physiological significance of its role in apoptosis is unclear. May play a role in the modulation of the response to osmotic stress by preventing NFAT5 to translocate into the nucleus and activate its target genes expression.^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

FSP27 (CIDE-3 in humans) plays critical roles in lipid metabolism and apoptosis and is known to be involved in regulation of lipid droplet (LD) size and lipid storage and apoptotic DNA fragmentation. Given that CIDE-containing proteins including FSP27 are associated with many human diseases including cancer, aging, diabetes, and obesity, studies of FSP27 and other CIDE-containing proteins are of great biological importance. As a first step toward elucidating the molecular mechanisms of FSP27-mediated lipid droplet growth and apoptosis, we report the crystal structure of the CIDE-N domain of FSP27 at a resolution of 2.0 A. The structure revealed a possible biologically important homo-dimeric interface similar to that formed by the hetero-dimeric complex, CAD/ICAD. Comparison with other structural homologues revealed that the PB1 domain of BEM1P, ubiquitin-like domain of BAG6 and ubiquitin are structurally similar proteins. Our homo-dimeric structure of the CIDE-N domain of FSP27 will provide important information that will enable better understanding of the function of FSP27.

Molecular basis for homo-dimerization of the CIDE domain revealed by the crystal structure of the CIDE-N domain of FSP27.,Lee SM, Jang TH, Park HH Biochem Biophys Res Commun. 2013 Oct 4;439(4):564-9. doi:, 10.1016/j.bbrc.2013.09.018. Epub 2013 Sep 8. PMID:24025675^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Keller P, Petrie JT, De Rose P, Gerin I, Wright WS, Chiang SH, Nielsen AR, Fischer CP, Pedersen BK, MacDougald OA. Fat-specific protein 27 regulates storage of triacylglycerol. J Biol Chem. 2008 May 23;283(21):14355-65. doi: 10.1074/jbc.M708323200. Epub 2008, Mar 11. PMID:18334488 doi:http://dx.doi.org/10.1074/jbc.M708323200
↑ Gong J, Sun Z, Wu L, Xu W, Schieber N, Xu D, Shui G, Yang H, Parton RG, Li P. Fsp27 promotes lipid droplet growth by lipid exchange and transfer at lipid droplet contact sites. J Cell Biol. 2011 Dec 12;195(6):953-63. doi: 10.1083/jcb.201104142. Epub 2011 Dec, 5. PMID:22144693 doi:http://dx.doi.org/10.1083/jcb.201104142
↑ Wang W, Lv N, Zhang S, Shui G, Qian H, Zhang J, Chen Y, Ye J, Xie Y, Shen Y, Wenk MR, Li P. Cidea is an essential transcriptional coactivator regulating mammary gland secretion of milk lipids. Nat Med. 2012 Jan 15;18(2):235-43. doi: 10.1038/nm.2614. PMID:22245780 doi:http://dx.doi.org/10.1038/nm.2614
↑ Sun Z, Gong J, Wu H, Xu W, Wu L, Xu D, Gao J, Wu JW, Yang H, Yang M, Li P. Perilipin1 promotes unilocular lipid droplet formation through the activation of Fsp27 in adipocytes. Nat Commun. 2013;4:1594. doi: 10.1038/ncomms2581. PMID:23481402 doi:http://dx.doi.org/10.1038/ncomms2581
↑ Lee SM, Jang TH, Park HH. Molecular basis for homo-dimerization of the CIDE domain revealed by the crystal structure of the CIDE-N domain of FSP27. Biochem Biophys Res Commun. 2013 Oct 4;439(4):564-9. doi:, 10.1016/j.bbrc.2013.09.018. Epub 2013 Sep 8. PMID:24025675 doi:http://dx.doi.org/10.1016/j.bbrc.2013.09.018

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4mac"

Categories: Large Structures | Mus musculus | Lee SM | Park HH

@@ Line 3: / Line 3: @@
 <StructureSection load='4mac' size='340' side='right'caption='[[4mac]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4mac]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MAC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MAC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4mac]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MAC FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Cidec, Fsp27 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4mac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mac OCA], [https://pdbe.org/4mac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mac RCSB], [https://www.ebi.ac.uk/pdbsum/4mac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mac ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mac OCA], [http://pdbe.org/4mac PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mac RCSB], [http://www.ebi.ac.uk/pdbsum/4mac PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mac ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CIDEC_MOUSE CIDEC_MOUSE]] Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair. Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1. May act as a CEBPB coactivator in the white adipose tissue to control the expression of a subset of CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment. As mature adipocytes, that express high CIDEC levels, are quite resistant to apoptotic stimuli, the physiological significance of its role in apoptosis is unclear. May play a role in the modulation of the response to osmotic stress by preventing NFAT5 to translocate into the nucleus and activate its target genes expression.<ref>PMID:18334488</ref> <ref>PMID:22144693</ref> <ref>PMID:22245780</ref> <ref>PMID:23481402</ref>
+[https://www.uniprot.org/uniprot/CIDEC_MOUSE CIDEC_MOUSE] Binds to lipid droplets and regulates their enlargement, thereby restricting lipolysis and favoring storage. At focal contact sites between lipid droplets, promotes directional net neutral lipid transfer from the smaller to larger lipid droplets. The transfer direction may be driven by the internal pressure difference between the contacting lipid droplet pair. Its role in neutral lipid transfer and lipid droplet enlargement is activated by the interaction with PLIN1. May act as a CEBPB coactivator in the white adipose tissue to control the expression of a subset of CEBPB downstream target genes, including SOCS1, SOCS3, TGFB1, TGFBR1, ID2 and XDH. When overexpressed in preadipocytes, induces apoptosis or increases cell susceptibility to apoptosis induced by serum deprivation or TGFB treatment. As mature adipocytes, that express high CIDEC levels, are quite resistant to apoptotic stimuli, the physiological significance of its role in apoptosis is unclear. May play a role in the modulation of the response to osmotic stress by preventing NFAT5 to translocate into the nucleus and activate its target genes expression.<ref>PMID:18334488</ref> <ref>PMID:22144693</ref> <ref>PMID:22245780</ref> <ref>PMID:23481402</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 22: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Lee, S M]]
+[[Category: Lee SM]]
-[[Category: Park, H H]]
+[[Category: Park HH]]
-[[Category: Apoptosis]]
-[[Category: Perilipin1]]
-[[Category: Protein interaction]]
-[[Category: Roll fold]]

4mac

From Proteopedia

Revision as of 11:05, 21 December 2022

Crystal structure of CIDE-N domain of FSP27

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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