Inheritance of the Golgi Apparatus and Cytokinesis Are Controlled by Degradation of GBF1

TY - JOUR

T1 - Inheritance of the Golgi Apparatus and Cytokinesis Are Controlled by Degradation of GBF1

AU - Magliozzi, Roberto

AU - Carrero, Zunamys I

AU - Low, Teck Yew

AU - Yuniati, Laurensia

AU - Valdes-Quezada, Christian

AU - Kruiswijk, Flore

AU - van Wijk, Koen

AU - Heck, Albert J R

AU - Jackson, Catherine L

AU - Guardavaccaro, Daniele

N1 - Copyright © 2018 The Authors. Published by Elsevier Inc. All rights reserved.

PY - 2018/6/12

Y1 - 2018/6/12

N2 - Although much is known about how chromosome segregation is coupled to cell division, how intracellular organelles partition during mitotic division is poorly understood. We report that the phosphorylation-dependent degradation of the ARFGEF GBF1 regulates organelle trafficking during cell division. We show that, in mitosis, GBF1 is phosphorylated on Ser292 and Ser297 by casein kinase-2 allowing recognition by the F-box protein βTrCP. GBF1 interaction with βTrCP recruits GBF1 to the SCFβTrCP ubiquitin ligase complex, triggering its degradation. Phosphorylation and degradation of GBF1 occur along microtubules at the intercellular bridge of telophase cells and are required for Golgi membrane positioning and postmitotic Golgi reformation. Indeed, expression of a non-degradable GBF1 mutant inhibits the transport of the Golgi cluster adjacent to the midbody toward the Golgi twin positioned next to the centrosome and results in defective Golgi reassembly and cytokinesis failure. These findings define a mechanism that controls postmitotic Golgi reassembly and inheritance.

AB - Although much is known about how chromosome segregation is coupled to cell division, how intracellular organelles partition during mitotic division is poorly understood. We report that the phosphorylation-dependent degradation of the ARFGEF GBF1 regulates organelle trafficking during cell division. We show that, in mitosis, GBF1 is phosphorylated on Ser292 and Ser297 by casein kinase-2 allowing recognition by the F-box protein βTrCP. GBF1 interaction with βTrCP recruits GBF1 to the SCFβTrCP ubiquitin ligase complex, triggering its degradation. Phosphorylation and degradation of GBF1 occur along microtubules at the intercellular bridge of telophase cells and are required for Golgi membrane positioning and postmitotic Golgi reformation. Indeed, expression of a non-degradable GBF1 mutant inhibits the transport of the Golgi cluster adjacent to the midbody toward the Golgi twin positioned next to the centrosome and results in defective Golgi reassembly and cytokinesis failure. These findings define a mechanism that controls postmitotic Golgi reassembly and inheritance.

U2 - 10.1016/j.celrep.2018.05.031

DO - 10.1016/j.celrep.2018.05.031

M3 - Article

C2 - 29898406

SN - 2211-1247

VL - 23

SP - 3381-3391.e4

JO - Cell Reports

JF - Cell Reports

IS - 11

ER -