SEC16A

Last update 08 May 2025

Basic Info

Synonyms

KIAA0310, p250, Protein transport protein Sec16A

+ [5]

Introduction

Acts as a molecular scaffold that plays a key role in the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining an ERES. Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:17005010, PubMed:17192411, PubMed:17428803, PubMed:21768384, PubMed:22355596). Mediates the recruitment of MIA3/TANGO to ERES (PubMed:28442536). Regulates both conventional (ER/Golgi-dependent) and GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane (PubMed:28067262). Positively regulates the protein stability of E3 ubiquitin-protein ligases RNF152 and RNF183 and the ER localization of RNF183 (PubMed:29300766). Acts as a RAB10 effector in the regulation of insulin-induced SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the cell membrane in adipocytes (By similarity).

100 Clinical Results associated with SEC16A

100 Translational Medicine associated with SEC16A

0 Patents (Medical) associated with SEC16A

115

Literatures (Medical) associated with SEC16A

01 Mar 2025·Journal of Cell Science

Potential ER tubular lumen sensing by intrinsically disordered regions

Article

Author: Yorimitsu, Tomohiro ; Sato, Ken

ABSTRACTIntrinsically disordered regions (IDRs) are known to sense the positive membrane curvature of vesicles and tubules. However, whether IDRs can sense the negative curvature of their luminal surfaces remains elusive. Here, we show that IDRs direct specific localization to endoplasmic reticulum (ER) tubules. In Saccharomyces cerevisiae, Sed4 interacts with Sec16 at the ER exit site (ERES) to promote ER export. Upon loss of this interaction, Sed4 failed to assemble at the ERES but was enriched in the ER tubules in a luminal region-dependent manner. Fusion of the Sed4 luminal region with Sec12 and Sec22, which localize throughout the ER, resulted in their enrichment in the tubules. The luminal regions of Sed4 or its homologs, predicted to be IDRs, localized to tubules when translocated alone into the ER lumen. The lumen-imported IDRs derived from cytosol-localizing Sec16 and Atg13 also exhibited tubule localization. Furthermore, Sed4 constructs in which the luminal region was replaced by these IDRs were concentrated at the ERES. Collectively, we suggest that the IDRs sense the properties of the tubule lumen, such as its surface, and facilitate Sed4 assembly at the ERES.

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.

02 Dec 2024·Plant Physiology

Functional diversification of Sec13 isoforms for storage protein trafficking in rice endosperm cells

Article

Author: Duan, Erchao ; Ren, Yulong ; Wang, Yihua ; Zhang, Pengcheng ; Wan, Gexing ; Wang, Yongfei ; Yang, Wenkun ; Zhao, Wenjie ; Teng, Xuan ; Liu, Shijia ; Zhang, Yu ; Pan, Tian ; Wang, Fan ; Zhang, Binglei ; Wan, Jianmin ; Lei, Cailin ; Han, Xiaohang ; Zhu, Shanshan ; Sun, Xiejun ; Zhu, Yun ; Chen, Yanyu ; Wang, Xin ; Chen, Yu

AbstractCoat protein complex II (COPII) vesicles play crucial roles in mediating the endoplasmic reticulum (ER) exit of newly synthesized proteins to the Golgi in eukaryotic cells. However, the molecular functions of COPII components and their functional diversifications in plant seeds remain obscure. Here, we showed that the rice (Oryza sativa) glutelin precursor accumulation12 (gpa12) mutant is defective in storage protein export from the ER, resulting in the formation of aggregated protein bodies. Map-based cloning revealed that GPA12 encodes a COPII outer layer protein, Sec13a, that mainly localizes to endoplasmic reticulum exit sites (ERES) and partially localizes to the Golgi. Biochemical experiments verified that Sec13a physically interacts with Sec31 and Sec16, and mutation in Sec13 compromises its interaction with Sec31 and Sec16, thereby affecting the membrane association of the inner complex components Sar1b and Sec23c. Apart from Sec13a, the rice genome encodes 2 other Sec13 isoforms, Sec13b and Sec13c. Notably, we observed an abnormal accumulation of globular ER structures in the sec13bc double mutant but not in the single mutants, suggesting a functional redundancy of Sec13b and Sec13c in modulating ER morphology. Taken together, our results substantiated that Sec13a plays an important role in regulating storage protein export from the ER, while Sec13b and Sec13c are required for maintaining ER morphology in rice endosperm cells. Our findings provide insights into the functional diversification of COPII components in plants.

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SEC16A

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