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Comment
. 2017 Feb;216(2):299-301.
doi: 10.1083/jcb.201612026. Epub 2017 Jan 25.

Vps13 and Cdc31/centrin: Puzzling partners in membrane traffic

Margaret D Myers  1 , Gregory S Payne  2
Affiliations
Comment

Vps13 and Cdc31/centrin: Puzzling partners in membrane traffic

Margaret D Myers et al. J Cell Biol. 2017 Feb.

Abstract

Yeast Vps13 is a member of a conserved protein family that includes human homologues associated with neurodegenerative and developmental disorders. In this issue, De et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201606078) establish direct roles for Vps13 and its surprising binding partner, the calcium-binding centrin Cdc31, in trans-Golgi network (TGN) to endosome traffic and TGN homotypic fusion.

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Figures

Figure 1.
Figure 1.
Myriad roles of Vps13 family members. De et al. (2017) reveal the architecture of yeast Vps13 (center) and define roles with Cdc31 in TGN to PVC traffic and TGN homotypic fusion (red arrow). Other arrows indicate functions associated with Vps13 in yeast (sporulation, mitochondrial integrity, and organelle junctions), humans (mitochondrial integrity, actin dynamics, autophagy, and Golgi organization), Dictyosteleum discoideum (autophagy), and Tetrahymena thermophila (phagocytosis). Human disorders caused by mutations in VPS13 genes are shown in the dark green oval. VPS13D has not been linked to human disease. The Vps13 image was originally published by De et al. (2017).
See this image and copyright information in PMC

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