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

Saegusa, Keiko; Matsunaga, Kohichi; Maeda, Miharu; Saito, Kota; Izumi, Tetsuro; Sato, Ken

doi:10.1038/s42003-022-03417-6

Cited by 28 publications

(18 citation statements)

References 59 publications

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“…elegans lipoproteins that share about 22% sequence identity with human apolipoprotein B (APOB); this same group demonstrated that SURF4 also serves as a cargo receptor for APOB in human hepatic HepG2 cells ( 162 ). Several other SURF4 cargoes have been identified, including growth hormone, dentin sialophosphoprotein (DSPP), amelogenin ( 163 ), erythropoietin ( 164 ), pathogenic A1AT polymers ( 165 ), sonic hedgehog ( 166 ), proinsulin ( 167 ), and the lysosomal proteins progranulin and prosaposin ( 168 ).…”

Section: Specificity Of Cargo Receptorsmentioning

confidence: 99%

Cargo selection in endoplasmic reticulum–to–Golgi transport and relevant diseases

Tang¹,

Ginsburg²

2023

Journal of Clinical Investigation

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Most proteins destined for the extracellular space or various intracellular compartments must traverse the intracellular secretory pathway. The first step is the recruitment and transport of cargoes from the endoplasmic reticulum (ER) lumen to the Golgi apparatus by coat protein complex II (COPII), consisting of five core proteins. Additional ER transmembrane proteins that aid cargo recruitment are referred to as cargo receptors. Gene duplication events have resulted in multiple COPII paralogs present in the mammalian genome. Here, we review the functions of each COPII protein, human disorders associated with each paralog, and evidence for functional conservation between paralogs. We also provide a summary of current knowledge regarding two prototypical cargo receptors in mammals, LMAN1 and SURF4, and their roles in human health and disease.

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Section: Specificity Of Cargo Receptorsmentioning

confidence: 99%

Cargo selection in endoplasmic reticulum–to–Golgi transport and relevant diseases

Tang¹,

Ginsburg²

2023

Journal of Clinical Investigation

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“…Surf4 has been implicated in ER export of diverse cargos, such as EPO, α1AT, and proinsulin ( Lin et al., 2020 ; Ordonez et al., 2021 ; Saegusa et al., 2022 ). EPO is mainly secreted into the blood by interstitial cells in the peritubular capillary bed of the renal cortex.…”

Section: Surf4 a Highly Conserved Cargo Receptormentioning

confidence: 99%

“…(2021) reported that Surf4 mediated ER–Golgi transport of both α1AT monomer and polymer in CHO cells, with a preference for the polymer. In addition, Saegusa et al. (2022) reported that Surf4 directly interacted with proinsulin and mediated the transport of proinsulin from the ER to the Golgi apparatus in cultured rat pancreatic beta cells.…”

Section: Surf4 a Highly Conserved Cargo Receptormentioning

confidence: 99%

“…Furthermore, they observed that Surf4 was localized in ERES, and Surf4 silencing reduced COPII-positive ERES in HepG2 cells, indicating its important role in maintaining ERES organization and protein export from the ER. Indeed, it has been reported that Surf4 facilitates secretion of various substrates, such as proinsulin ( Saegusa et al., 2022 ), prosaposin ( Devireddy and Ferguson, 2022 ), and EPO ( Lin et al., 2020 ). On other hand, Mitrovic et al.…”

Section: Surf4 a Highly Conserved Cargo Receptormentioning

confidence: 99%

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Surf4, cargo trafficking, lipid metabolism, and therapeutic implications

Shen

Qin

et al. 2022

Journal of Molecular Cell Biology

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Surfeit 4 is a polytopic transmembrane protein that primarily resides in the endoplasmic reticulum (ER) membrane. It is ubiquitously expressed and functions as a cargo receptor, mediating cargo transport from the ER and the Golgi apparatus via the canonical coat protein complex II (COPII)-coated vesicles or specific vesicles. It also participates in ER–Golgi protein trafficking through a tubular network. Meanwhile, it facilitates retrograde transportation of cargos from the Golgi apparatus to the ER through COPI-coated vesicles. Surf4 can selectively mediate export of diverse cargos, such as proprotein convertase subtilisin/kexin type 9 (PCSK9), very low-density lipoprotein (VLDL), progranulin, α1-antitrypsin, STING, proinsulin, and erythropoietin. It has been implicated in facilitating VLDL secretion, promoting cell proliferation and migration, and increasing replication of positive-strand RNA viruses. Therefore, Surf4 plays a crucial role in various physiological and pathophysiological processes and emerges as a promising therapeutic target. However, the molecular mechanisms by which Surf4 selectively sorts diverse cargos for ER–Golgi protein trafficking remain elusive. Here, we summarize the most recent advances in Surf4, focusing on its role in lipid metabolism.

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“…Indeed, ERES size and number have been shown to increase with elevated secretory load (Farhan et al, 2008a). Specialized cell types with high biosynthetic and secretory capacities can display dozens to hundreds of ERESs, while simpler cells can display as few as a single ERES (Saegusa et al, 2022; Stephens, 2003; Warren, 2013; Yelinek et al, 2009). In Drosophila neurons, genes involved in ERES function have been shown to play an important role in dendritic arbor development (Ye et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Neurons alter endoplasmic reticulum exit sites to accommodate dendritic arbor size

Land

Fetter

Liang

et al. 2022

Preprint

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Nervous systems exhibit dramatic diversity in cell morphology and size. How neurons regulate their biosynthetic and secretory machinery to support different cell sizes is not well understood. Endoplasmic reticulum exit sites (ERESs) are essential for maintaining secretory flux, and are required for normal dendrite development.1However, it is unknown how neurons of different size regulate the number of secretory structures to accommodate morphogenesis. InC. elegans, we find that ERES number is strongly correlated with the size of a neuron's dendritic arbor. The elaborately branched sensory neuron, PVD, has especially high ERES numbers in its soma. PVD establishes its high ERES number rapidly after birth, actively maintains ERES number as PVD grows and matures. The initial high number of ERES in PVD is driven by asymmetric cell division producing a large cell size at birth. Subsequent maintenance of ERES number requires the cell fate transcription factor MEC-3 andC. elegansTOR (ceTOR/let-363). ThisceTOR/let-363pathway integrates nutrient availability to coordinate ERES number with soma size and dendritic expansion. Our results are consistent with a model in which transcription factors, master metabolic regulators and nutrient availability coordinate to specify developmental parameters including soma size, ERES number and dendrite size, which together determine neuronal cell fate.

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

Cited by 28 publications

References 59 publications

Cargo selection in endoplasmic reticulum–to–Golgi transport and relevant diseases

Cargo selection in endoplasmic reticulum–to–Golgi transport and relevant diseases

Surf4, cargo trafficking, lipid metabolism, and therapeutic implications

Neurons alter endoplasmic reticulum exit sites to accommodate dendritic arbor size

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