A phosphorylation switch regulates RAB6 function during mitosis
Jimenez, A. J.; Bousquet, H.; Bardin, S.; Perez, F.; Goud, B.; Miserey, S.
Show abstract
RAB GTPases are key regulators of membrane trafficking in eukaryotic cells. In addition to their role in interphase, several RAB proteins, including Golgi-associated RAB6, have mitotic functions. The aim of this study was to investigate how the interphasic and mitotic functions of RAB6 could be regulated. Since phosphorylation is a key regulatory process in mitosis, we looked for specific mitotic phosphorylation of RAB6 using a phospho-proteomic approach. We found that RAB6 is phosphorylated at position S52 by the mitotic kinase Pololike kinase 1 (Plk1) in mitosis. Phosphorylated RAB6 localizes at the spindle poles from prophase to anaphase. In metaphase, we observed RAB6A-positive structures containing Mad1 and Mad2 moving along the mitotic spindle via the dynein-dynactin complex. We provide evidence that phosphorylation impairs RAB6A binding to some of its known partners, including p150Glued and Bicaudal-D2. In addition, the overexpression of RAB6A phospho-mutants lead to mitosis and cytokinesis defects. Our results suggest that a cycle of RAB6 phosphorylation/dephosphorylation is required for cell division.
Matching journals
The top 3 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Defining endogenous TACC3-chTOG-clathrin-GTSE1 interactions at the mitotic spindle using induced relocalization 96%
- RBD11, a bioengineered Rab11-binding module for visualizing and analyzing endogenous Rab11 95%
- Atypical small GTPase RABL3 interacts with RAB11 to regulate early ciliogenesis in human cells 95%
Similar papers in this journal
Similar papers in this journal
- Augmin prevents merotelic attachments by promoting proper arrangement of bridging and kinetochore fibers 95%
- Concerted action of kinesins KIF5B and KIF13B promotes efficient secretory vesicle transport to microtubule plus ends 94%
- A Feed-forward Pathway Drives LRRK2 kinase Membrane Recruitment and Activation 94%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.