TY - JOUR
T1 - VPS13B is localized at the interface between Golgi cisternae and is a functional partner of FAM177A1
AU - Ugur, Berrak
AU - Schueder, Florian
AU - Shin, Jimann
AU - Hanna, Michael G.
AU - Wu, Yumei
AU - Leonzino, Marianna
AU - Su, Maohan
AU - McAdow, Anthony R.
AU - Wilson, Catherine
AU - Postlethwait, John
AU - Solnica-Krezel, Lilianna
AU - Bewersdorf, Joerg
AU - De Camilli, Pietro
N1 - Publisher Copyright:
© 2024 Ugur et al.
PY - 2024/12/2
Y1 - 2024/12/2
N2 - Mutations in VPS13B, a member of a protein family implicated in bulk lipid transport between adjacent membranes, cause Cohen syndrome. VPS13B is known to be concentrated in the Golgi complex, but its precise location within this organelle and thus the site(s) where it achieves lipid transport remains unclear. Here, we show that VPS13B is localized at the interface between proximal and distal Golgi subcompartments and that Golgi complex reformation after Brefeldin A (BFA)-induced disruption is delayed in VPS13B KO cells. This delay is phenocopied by the loss of FAM177A1, a Golgi complex protein of unknown function reported to be a VPS13B interactor and whose mutations also result in a developmental disorder. In zebrafish, the vps13b ortholog, not previously annotated in this organism, genetically interacts with fam177a1. Collectively, these findings raise the possibility that bulk lipid transport by VPS13B may play a role in the dynamics of Golgi membranes and that VPS13B may be assisted in this function by FAM177A1.
AB - Mutations in VPS13B, a member of a protein family implicated in bulk lipid transport between adjacent membranes, cause Cohen syndrome. VPS13B is known to be concentrated in the Golgi complex, but its precise location within this organelle and thus the site(s) where it achieves lipid transport remains unclear. Here, we show that VPS13B is localized at the interface between proximal and distal Golgi subcompartments and that Golgi complex reformation after Brefeldin A (BFA)-induced disruption is delayed in VPS13B KO cells. This delay is phenocopied by the loss of FAM177A1, a Golgi complex protein of unknown function reported to be a VPS13B interactor and whose mutations also result in a developmental disorder. In zebrafish, the vps13b ortholog, not previously annotated in this organism, genetically interacts with fam177a1. Collectively, these findings raise the possibility that bulk lipid transport by VPS13B may play a role in the dynamics of Golgi membranes and that VPS13B may be assisted in this function by FAM177A1.
UR - http://www.scopus.com/inward/record.url?scp=85205151829&partnerID=8YFLogxK
U2 - 10.1083/jcb.202311189
DO - 10.1083/jcb.202311189
M3 - Article
C2 - 39331042
AN - SCOPUS:85205151829
SN - 0021-9525
VL - 223
JO - The Journal of cell biology
JF - The Journal of cell biology
IS - 12
ER -