Cargo receptor Surf4 regulates endoplasmic reticulum export of proinsulin in pancreatic β-cells

Insulin is an essential peptide hormone that maintains blood glucose levels. Although the mechanisms underlying insulin exocytosis have been investigated, the mechanism of proinsulin export from the endoplasmic reticulum (ER) remains unclear. Here, we demonstrated that Surf4, a cargo receptor homolo...

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Published inCommunications biology Vol. 5; no. 1; p. 458
Main Authors Saegusa, Keiko, Matsunaga, Kohichi, Maeda, Miharu, Saito, Kota, Izumi, Tetsuro, Sato, Ken
Format Journal Article
LanguageEnglish
Published England Nature Publishing Group 13.05.2022
Nature Publishing Group UK
Nature Portfolio
Subjects
Beta cells
Biology
Blood glucose
Endoplasmic reticulum
Exocytosis
Glucose
Insulin
Insulin secretion
Insulinoma
Pancreas
Secretion
Secretory vesicles
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Abstract Insulin is an essential peptide hormone that maintains blood glucose levels. Although the mechanisms underlying insulin exocytosis have been investigated, the mechanism of proinsulin export from the endoplasmic reticulum (ER) remains unclear. Here, we demonstrated that Surf4, a cargo receptor homolog, regulates the ER export of proinsulin via its recruitment to ER exit sites (ERES). Under high-glucose conditions, Surf4 expression was upregulated, and Surf4 proteins mainly localized to the ER at a steady state and accumulated in the ERES, along with proinsulin in rat insulinoma INS-1 cells. Surf4-knockdown resulted in proinsulin retention in the ER and decreased the levels of mature insulin in secretory granules, thereby significantly reducing insulin secretion. Surf4 forms an oligomer and can physically interact with proinsulin and Sec12, essential for COPII vesicle formation. Our findings suggest that Surf4 interacts with proinsulin and delivers it into COPII vesicles for ER export in co-operation with Sec12 and COPII.
AbstractList Abstract Insulin is an essential peptide hormone that maintains blood glucose levels. Although the mechanisms underlying insulin exocytosis have been investigated, the mechanism of proinsulin export from the endoplasmic reticulum (ER) remains unclear. Here, we demonstrated that Surf4, a cargo receptor homolog, regulates the ER export of proinsulin via its recruitment to ER exit sites (ERES). Under high-glucose conditions, Surf4 expression was upregulated, and Surf4 proteins mainly localized to the ER at a steady state and accumulated in the ERES, along with proinsulin in rat insulinoma INS-1 cells. Surf4 -knockdown resulted in proinsulin retention in the ER and decreased the levels of mature insulin in secretory granules, thereby significantly reducing insulin secretion. Surf4 forms an oligomer and can physically interact with proinsulin and Sec12, essential for COPII vesicle formation. Our findings suggest that Surf4 interacts with proinsulin and delivers it into COPII vesicles for ER export in co-operation with Sec12 and COPII.
Insulin is an essential peptide hormone that maintains blood glucose levels. Although the mechanisms underlying insulin exocytosis have been investigated, the mechanism of proinsulin export from the endoplasmic reticulum (ER) remains unclear. Here, we demonstrated that Surf4, a cargo receptor homolog, regulates the ER export of proinsulin via its recruitment to ER exit sites (ERES). Under high-glucose conditions, Surf4 expression was upregulated, and Surf4 proteins mainly localized to the ER at a steady state and accumulated in the ERES, along with proinsulin in rat insulinoma INS-1 cells. Surf4-knockdown resulted in proinsulin retention in the ER and decreased the levels of mature insulin in secretory granules, thereby significantly reducing insulin secretion. Surf4 forms an oligomer and can physically interact with proinsulin and Sec12, essential for COPII vesicle formation. Our findings suggest that Surf4 interacts with proinsulin and delivers it into COPII vesicles for ER export in co-operation with Sec12 and COPII.
Surf4 is an ER cargo receptor for proinsulin, facilitating proinsulin export out of the ERES in a cellular model of pancreatic β-cells, with its expression dependent on glucose concentration and Surf4 knockdown impairing insulin secretion.
Insulin is an essential peptide hormone that maintains blood glucose levels. Although the mechanisms underlying insulin exocytosis have been investigated, the mechanism of proinsulin export from the endoplasmic reticulum (ER) remains unclear. Here, we demonstrated that Surf4, a cargo receptor homolog, regulates the ER export of proinsulin via its recruitment to ER exit sites (ERES). Under high-glucose conditions, Surf4 expression was upregulated, and Surf4 proteins mainly localized to the ER at a steady state and accumulated in the ERES, along with proinsulin in rat insulinoma INS-1 cells. Surf4-knockdown resulted in proinsulin retention in the ER and decreased the levels of mature insulin in secretory granules, thereby significantly reducing insulin secretion. Surf4 forms an oligomer and can physically interact with proinsulin and Sec12, essential for COPII vesicle formation. Our findings suggest that Surf4 interacts with proinsulin and delivers it into COPII vesicles for ER export in co-operation with Sec12 and COPII.Surf4 is an ER cargo receptor for proinsulin, facilitating proinsulin export out of the ERES in a cellular model of pancreatic β-cells, with its expression dependent on glucose concentration and Surf4 knockdown impairing insulin secretion.
Insulin is an essential peptide hormone that maintains blood glucose levels. Although the mechanisms underlying insulin exocytosis have been investigated, the mechanism of proinsulin export from the endoplasmic reticulum (ER) remains unclear. Here, we demonstrated that Surf4, a cargo receptor homolog, regulates the ER export of proinsulin via its recruitment to ER exit sites (ERES). Under high-glucose conditions, Surf4 expression was upregulated, and Surf4 proteins mainly localized to the ER at a steady state and accumulated in the ERES, along with proinsulin in rat insulinoma INS-1 cells. Surf4 -knockdown resulted in proinsulin retention in the ER and decreased the levels of mature insulin in secretory granules, thereby significantly reducing insulin secretion. Surf4 forms an oligomer and can physically interact with proinsulin and Sec12, essential for COPII vesicle formation. Our findings suggest that Surf4 interacts with proinsulin and delivers it into COPII vesicles for ER export in co-operation with Sec12 and COPII. Surf4 is an ER cargo receptor for proinsulin, facilitating proinsulin export out of the ERES in a cellular model of pancreatic β-cells, with its expression dependent on glucose concentration and Surf4 knockdown impairing insulin secretion.
ArticleNumber 458
Author Maeda, Miharu
Saito, Kota
Saegusa, Keiko
Izumi, Tetsuro
Matsunaga, Kohichi
Sato, Ken
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  organization: Gunma University, Initiative for Advanced Research (GIAR), Gunma, 371-8512, Japan. sato-ken@gunma-u.ac.jp
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Snippet Insulin is an essential peptide hormone that maintains blood glucose levels. Although the mechanisms underlying insulin exocytosis have been investigated, the...
Abstract Insulin is an essential peptide hormone that maintains blood glucose levels. Although the mechanisms underlying insulin exocytosis have been...
Surf4 is an ER cargo receptor for proinsulin, facilitating proinsulin export out of the ERES in a cellular model of pancreatic β-cells, with its expression...
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StartPage 458
SubjectTerms Beta cells
Biology
Blood glucose
Endoplasmic reticulum
Exocytosis
Glucose
Insulin
Insulin secretion
Insulinoma
Pancreas
Secretion
Secretory vesicles
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Title Cargo receptor Surf4 regulates endoplasmic reticulum export of proinsulin in pancreatic β-cells
URI https://www.ncbi.nlm.nih.gov/pubmed/35562580
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