Oct 25, 2018

cTAGE5 acts as a Sar1 GTPase regulator for collagen export

BioRxiv : the Preprint Server for Biology
Norito SasakiKota Saito

Abstract

Secretory proteins synthesized within the endoplasmic reticulum (ER) are exported via coat protein complex II (COPII)-coated vesicles. The formation of the COPII-coated vesicles is initiated by activation of the small GTPase, Sar1. cTAGE5 directly interacts with a guanine-nucleotide exchange factor (GEF), Sec12, and a GTPase-activating protein (GAP) of Sar1, Sec23. We have previously shown that cTAGE5 recruits Sec12 to the ER exit sites for efficient production of activated Sar1 for collagen secretion. However, the functional significance of the interaction between cTAGE5 and Sec23 has not been fully elucidated. In this study, we showed that cTAGE5 enhances the GAP activity of Sec23 toward Sar1. In addition, the interaction of cTAGE5 with Sec23 is necessary for collagen exit from the ER. Our data suggests that cTAGE5 acts as a Sar1 GTPase regulator for collagen secretion.

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Mentioned in this Paper

Guanine
Study
IQGAP1
CTAGE5 protein, human
RASA1 gene
Guanyl-nucleotide Exchange Factor Activity
Sec23a protein, mouse
Ras GTPase-Activating Protein 1
Process of Secretion
PREB gene

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