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Last update 08 May 2025

SEC23A

Last update 08 May 2025

Basic Info

Synonyms

hSec23A, Protein transport protein Sec23A, SEC23 homolog A, COPII coat complex component

+ [2]

Introduction

Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex. Required for the translocation of insulin-induced glucose transporter SLC2A4/GLUT4 to the cell membrane (By similarity).

Drugs associated with SEC23A

RN-1(University of Michigan)

Target

KDM1A x SEC23A

Mechanism

KDM1A inhibitors [+1]

Active Org.

University of Michigan

Originator Org.

University of Michigan

Active Indication

Anemia, Dyserythropoietic, Congenital [+1]

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with SEC23A

100 Translational Medicine associated with SEC23A

0 Patents (Medical) associated with SEC23A

104

Literatures (Medical) associated with SEC23A

01 Apr 2025·Apoptosis

The impact of SEC23A on 5-FU chemotherapy sensitivity and its involvement in endoplasmic reticulum stress-induced apoptosis in colorectal cancer

Article

Author: Krohn, Mathias ; Schwarz, Sandra ; Su, Zhaoran ; Liu, Menglan ; Linnebacher, Michael

AbstractBackground: Colorectal cancer (CRC) represents a significant global health burden, with chemotherapy resistance representing a significant challenge to effective treatment. SEC23A, a core component of the COPII vesicle trafficking system, is of critical importance with regard to protein transport and cellular homeostasis. Nevertheless, its function in CRC progression and chemoresistance remains uncertain. The present study investigates the correlation between SEC23A expression and sensitivity to 5-fluorouracil (5-FU), a widely used chemotherapeutic agent, with particular emphasis on ER stress-induced apoptosis. Methods: A bioinformatic analysis was conducted to evaluate SEC23A expression in CRC and its association with patient prognosis. Chemotherapy sensitivity was predicted using GDSC data and validated experimentally using CRC cell lines with manipulated SEC23A expression. In order to explore the role of SEC23A in acquired drug resistance, patient-derived xenograft (PDX) models and 5-FU-resistant cell lines were employed. Apoptosis assays, cell cycle analysis, and ER stress modulation experiments were performed to elucidate the underlying mechanisms. Results: SEC23A expression was significantly reduced in CRC samples compared to normal tissues. This reduction was linked to a poorer prognosis, including both overall and disease-specific survival. A correlation was observed between low SEC23A expression and increased resistance to 5-FU, as evidenced by both bioinformatic predictions and in vitro experiments. In PDX models, metastatic lesions exhibited decreased SEC23A expression following 5-FU treatment in comparison to primary tumors. Overexpression of SEC23A in 5-FU-resistant cell lines restored sensitivity to the drug and increased apoptosis. Bioinformatic and experimental analyses revealed a robust correlation between SEC23A and ER stress-related apoptotic pathways. Elevated expression of SEC23A was observed to facilitate the accumulation of misfolded proteins in response to 5-FU treatment, which in turn resulted in increased ER stress and apoptosis. Conclusions: SEC23A plays a crucial role in modulating the sensitivity of CRC cells to 5-FU by regulating ER stress-induced apoptosis. Its downregulation contributes to chemoresistance, indicating that SEC23A may serve as a prognostic marker and therapeutic target in CRC. Strategies aimed at upregulating SEC23A or enhancing ER stress may provide new avenues for overcoming chemoresistance and improving treatment outcomes for CRC patients.

01 Mar 2025·Cancer Reports

Exploration of the Prognostic Markers of Multiple Myeloma Based on Cuproptosis‐Related Genes

Article

Author: Yuan, Jun ; Gao, Xiao‐Han ; Wang, Rui‐Cang ; Li, Yan ; Zhang, Xiao‐Xia ; Li, Jie ; Yang, Jie

ABSTRACTBackgroundThe investigation of cuproptosis in relation to tumor development has been limited, particularly in multiple myeloma (MM), indicating the need for further research. Our study aimed to examine the impact of cuproptosis‐related genes (CRGs) on the prognosis of MM.MethodsUsing the datasets, we filtered cuproptosis score‐related differentially expressed genes (CRDEGs) by overlapping the DEGs between the MM and normal groups and between the high and low cuproptosis score groups. Additionally, key module genes were identified through weighted gene co‐expression network analysis. A univariate Cox algorithm and multivariate Cox analysis were employed to obtain biomarkers of MM and build a prognostic model before conducting independent prognostic analysis.ResultsA total of 59 CRDEGs were filtered, demonstrating their involvement in the COPII vesicle coat and endoplasmic reticulum protein processing, and protein processing in the endoplasmic reticulum. Six prognosis‐related biomarkers (PARP1, EDEM3, SEC23A, RSL24D1, TTC37, and SRP72) were obtained, and a prognostic model was developed. The performance of the model was verified using a test cohort (GSE136324 dataset) and a validation cohort (GSE24080 dataset). Risk score, age, albumin, International Staging System (ISS) score, and β2‐microglobulin (B2M) were found to be significant predictors of prognosis independently.ConclusionAs a result of this investigation, a set of six biomarkers associated with cuproptosis (PARP1, EDEM3, SEC23A, RSL24D1, TTC37, and SRP72) were screened to provide a basis for predicting the prognosis of MM.

02 Jan 2025·Autophagy

Myotubularin 2 interacts with SEC23A and negatively regulates autophagy at ER exit sites in Arabidopsis

Article

Author: Gong, Qingqiu ; Bai, Fang ; Li, Xinjing ; Zheng, Jing ; Su, Jing ; Luan, Lin ; Wang, Lin ; Wang, Taotao ; Zhong, Qing

Starvation- or stress-induced phosphatidylinositol 3-phosphate (PtdIns3P/PI3P) production at the endoplasmic reticulum (ER) subdomains organizes phagophore assembly and autophagosome formation. Coat protein complex II (COPII) vesicles budding from ER exit site (ERES) also contribute to autophagosome formation. Whether any PtdIns3P phosphatase functions at ERES to inhibit macroautophagy/autophagy is unknown. Here we report Myotubularin 2 (MTM2) of Arabidopsis as a PtdIns3P phosphatase that localizes to ERES and negatively regulates autophagy. MTM2 binds PtdIns3P with its PH-GRAM domain in vitro and acts toward PtdIns3P in vivo. Transiently expressed MTM2 colocalizes with ATG14b, a subunit of the phosphatidylinositol 3-kinase (PtdIns3K) complex, and overexpression of MTM2 blocks autophagic flux and causes over-accumulation of ATG18a, ATG5, and ATG8a. The mtm2 mutant has higher levels of autophagy and is more tolerant to starvation, whereas MTM2 overexpression leads to reduced autophagy and sensitivity to starvation. The phenotypes of mtm2 are suppressed by ATG2 mutation, suggesting that MTM2 acts upstream of ATG2. Importantly, MTM2 does not affect the endosomal functions of PtdIns3P. Instead, MTM2 specifically colocalizes with COPII coat proteins and is cradled by the ERES-defining protein SEC16. MTM2 interacts with SEC23A with its phosphatase domain and inhibits COPII-mediated protein secretion. Finally, a role for MTM2 in salt stress response is uncovered. mtm2 resembles the halophyte Thellungiella salsuginea in its efficient vacuolar compartmentation of Na⁺, maintenance of chloroplast integrity, and timely regulation of autophagy-related genes. Our findings reveal a balance between PtdIns3P synthesis and turnover in autophagosome formation, and provide a new link between autophagy and COPII function.Abbreviations: ATG: autophagy related; BFA: brefeldin A; BiFC: bimolecular fluorescence complementation; CHX: cycloheximide; ConA: concanamycin A; COPII: coat protein complex II; ER: endoplasmic reticulum; ERES: ER exit site; MS: Murashige and Skoog; MTM: myotubularin; MVB: multivesicular body; PAS: phagophore assembly site; PI: phosphoinositide; TEM: transmission electron microscopy; WT: wild-type.

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