CK2 Phosphorylates Sec31 and Regulates ER-To-Golgi Trafficking

Mayuko Koreishi, Sidney Yu, Mayumi Oda, Yasuko Honjo, Ayano Satoh

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Protein export from the endoplasmic reticulum (ER) is an initial and rate-limiting step of molecular trafficking and secretion. This is mediated by coat protein II (COPII)-coated vesicles, whose formation requires small GTPase Sar1 and 6 Sec proteins including Sec23 and Sec31. Sec31 is a component of the outer layer of COPII coat and has been identified as a phosphoprotein. The initiation and promotion of COPII vesicle formation is regulated by Sar1; however, the mechanism regulating the completion of COPII vesicle formation followed by vesicle release is largely unknown. Hypothesizing that the Sec31 phosphorylation may be such a mechanism, we identified phosphorylation sites in the middle linker region of Sec31. Sec31 phosphorylation appeared to decrease its association with ER membranes and Sec23. Non-phosphorylatable mutant of Sec31 stayed longer at ER exit sites and bound more strongly to Sec23. We also found that CK2 is one of the kinases responsible for Sec31 phosphorylation because CK2 knockdown decreased Sec31 phosphorylation, whereas CK2 overexpression increased Sec31 phosphorylation. Furthermore, CK2 knockdown increased affinity of Sec31 for Sec23 and inhibited ER-to-Golgi trafficking. These results suggest that Sec31 phosphorylation by CK2 controls the duration of COPII vesicle formation, which regulates ER-to-Golgi trafficking.

Original languageEnglish
Article numbere54382
JournalPLoS One
Volume8
Issue number1
DOIs
Publication statusPublished - Jan 18 2013

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Phosphorylation
Endoplasmic Reticulum
endoplasmic reticulum
phosphorylation
Capsid Proteins
coat proteins
Coated Vesicles
coated vesicles
phosphoproteins
Monomeric GTP-Binding Proteins
Phosphoproteins
guanosinetriphosphatase
phosphotransferases (kinases)
Proteins
Phosphotransferases
proteins
Association reactions
secretion
Membranes
mutants

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

Cite this

CK2 Phosphorylates Sec31 and Regulates ER-To-Golgi Trafficking. / Koreishi, Mayuko; Yu, Sidney; Oda, Mayumi; Honjo, Yasuko; Satoh, Ayano.

In: PLoS One, Vol. 8, No. 1, e54382, 18.01.2013.

Research output: Contribution to journalArticle

Koreishi, Mayuko ; Yu, Sidney ; Oda, Mayumi ; Honjo, Yasuko ; Satoh, Ayano. / CK2 Phosphorylates Sec31 and Regulates ER-To-Golgi Trafficking. In: PLoS One. 2013 ; Vol. 8, No. 1.
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