Mitotic ER Exit Site Disassembly and Reassembly Are Regulated by the Phosphorylation Status of TANGO1

Golgi fragmentation and ER exit site disassembly are considered to be the leading causes of the mitotic block of secretion from the ER. Although the mechanisms of Golgi fragmentation have been extensively characterized, ER exit block early in mitosis is not well understood. We previously demonstrate...

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Bibliographic Details
Published in:Developmental cell 2020-10, Vol.55 (2), p.237-250.e5
Main Authors: Maeda, Miharu, Komatsu, Yukie, Saito, Kota
Format: Article
Language:English
Subjects:
Aryl Hydrocarbon Receptor Nuclear Translocator - metabolism
CK1
COPII
Endoplasmic Reticulum - metabolism
ER exit site
Golgi Apparatus - metabolism
HeLa Cells
Humans
mitosis
Mitosis - physiology
Phosphorylation - physiology
PP1
Protein Transport - physiology
Sec16
secretion
TANGO1
Vesicular Transport Proteins - metabolism
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Summary:Golgi fragmentation and ER exit site disassembly are considered to be the leading causes of the mitotic block of secretion from the ER. Although the mechanisms of Golgi fragmentation have been extensively characterized, ER exit block early in mitosis is not well understood. We previously demonstrated that TANGO1 organizes ER exit sites by directly interacting with Sec16. In this study, we identified TANGO1 as a regulator of ER exit site disassembly during mitosis. TANGO1 phosphorylation was observed to be coordinately regulated by a kinase (CK1) and a phosphatase (PP1). CK1-mediated TANGO1 phosphorylation reduces binding to Sec16, leading to the disassembly of ER exit sites. CK1 constantly phosphorylates TANGO1, whereas PP1-mediated dephosphorylation of TANGO1 decreases during mitosis. Thus, the phosphorylation status of TANGO1, which is controlled by balanced activities of the kinase CK1 and the phosphatase PP1, regulates the organization of ER exit sites during the cell cycle. [Display omitted] •TANGO1 phosphorylation is coordinately regulated by CK1 and PP1•CK1-mediated TANGO1 phosphorylation reduces the binding between Sec16 and TANGO1•TANGO1 phosphorylation is required for mitotic ER exit site disassembly The mechanism of ER exit site disassembly during mitosis is not well understood. Maeda et al. report that phosphorylation of TANGO1, which is controlled by balanced activities of the kinase CK1 and the phosphatase PP1, is required for ER exit site disassembly during mitosis.
ISSN:1534-5807
1878-1551
DOI:10.1016/j.devcel.2020.07.017