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Comment
. 2018 Oct 1;217(10):3322-3324.
doi: 10.1083/jcb.201808151. Epub 2018 Sep 4.

VPS13: A lipid transfer protein making contacts at multiple cellular locations

Mingming Gao  1 , Hongyuan Yang  2
Affiliations
Comment

VPS13: A lipid transfer protein making contacts at multiple cellular locations

Mingming Gao et al. J Cell Biol. .

Abstract

The evolutionarily conserved VPS13 proteins localize to multiple membrane contact sites though their function and regulation has been elusive. Bean et al. (2018. J. Cell Biol. https://doi.org/10.1083/jcb.201804111) found that competitive adaptors control the different localizations of yeast Vps13p, while Kumar et al. (2018. J. Cell Biol. https://doi.org/10.1083/jcb.201807019) provide biochemical and structural evidence for VPS13 proteins in the nonvesicular transport of phospholipids.

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Figures

Figure 1.
Figure 1.
Mammalian VPS13 proteins localize to different contact sites to mediate lipid transfer. (A) VPS13 proteins localize to different MCSs. LE/Lys: late endosome/lysosome; Mito, mitochondrion. (B) Hypothetical models of VPS13A function as an LTP. Through interacting with VAMP-associated protein (VAP) on the ER as well as lipids and putative adaptor proteins on the mitochondria outer membrane (MOM), VPS13A localizes to the ER–mitochondria contact site. Left: The N-terminal domain of VPS13A may form a hydrophobic tunnel connecting two membranes, allowing glycerophospholipids to “slide” through. Right: VPS13A may function as a large carrier, shuttling glycerophospholipids between membranes.
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References

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