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4IKG

Crystal structure of cell death-inducing DFFA-like effector c

Summary for 4IKG
Entry DOI10.2210/pdb4ikg/pdb
DescriptorCell death activator CIDE-3, IODIDE ION (3 entities in total)
Functional Keywordsfsp27, cell death, apoptosis
Biological sourceMus musculus (mouse)
Cellular locationLipid droplet: P56198
Total number of polymer chains1
Total formula weight9809.27
Authors
Yang, M.,Gao, J. (deposition date: 2012-12-26, release date: 2014-06-04, Last modification date: 2024-02-28)
Primary citationSun, Z.,Gong, J.,Wu, H.,Xu, W.,Wu, L.,Xu, D.,Gao, J.,Wu, J.W.,Yang, H.,Yang, M.,Li, P.
Perilipin1 promotes unilocular lipid droplet formation through the activation of Fsp27 in adipocytes.
Nat Commun, 4:1594-1594, 2013
Cited by
PubMed Abstract: Mature white adipocytes contain a characteristic unilocular lipid droplet. However, the molecular mechanisms underlying unilocular lipid droplet formation are poorly understood. We previously showed that Fsp27, an adipocyte-specific lipid droplet-associated protein, promotes lipid droplet growth by initiating lipid exchange and transfer. Here, we identify Perilipin1 (Plin1), another adipocyte-specific lipid droplet-associated protein, as an Fsp27 activator. Plin1 interacts with the CIDE-N domain of Fsp27 and markedly increases Fsp27-mediated lipid exchange, lipid transfer and lipid droplet growth. Functional cooperation between Plin1 and Fsp27 is required for efficient lipid droplet growth in adipocytes, as depletion of either protein impairs lipid droplet growth. The CIDE-N domain of Fsp27 forms homodimers and disruption of CIDE-N homodimerization abolishes Fsp27-mediated lipid exchange and transfer. Interestingly, Plin1 can restore the activity of CIDE-N homodimerization-defective mutants of Fsp27. We thus uncover a novel mechanism underlying lipid droplet growth and unilocular lipid droplet formation that involves the cooperative action of Fsp27 and Plin1 in adipocytes.
PubMed: 23481402
DOI: 10.1038/ncomms2581
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9318 Å)
Structure validation

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