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. Author manuscript; available in PMC: 2020 Dec 2.
Published in final edited form as: Dev Cell. 2019 Nov 7;51(5):551–563.e7. doi: 10.1016/j.devcel.2019.10.006

Figure 7. Model LD formation at LDAF1-seipin complex sites.

Figure 7.

Schematic representation of a model of how the LDAF1-seipin complex functions in LD formation in the ER. Oligomers of LDAF1 and seipin form a very large complex (~600 kDa) with as many as 66 transmembrane domains [11-mer of seipin (2x TMDs) + LDAF1 (2x double hairpins = 4 TMDs)] and 11 seipin hydrophobic helices in the ER bilayer. This assembly of hydrophobic helices may serve to promote nucleation and TG lens formation. TG accumulation in the complex causes dissociation of the complex and redistribution and translocation of LDAF1 to the growing LD surface as LDs grow. LDAF1 redistribution to LD surfaces may lower LD surface tension, aiding efficient budding and growth of LDs.