The p24 family of proteins have been regarded as cargo receptors for endoplasmic reticulum (ER) to Golgi transport; however, their precise functions have yet to be revealed. In this issue, Pastor-Pareja and colleagues (https://doi.org/10.1083/jcb.202309045) show that the interaction of these proteins with Tango1 is critical for their localization at the ER exit site (ERES) and efficient transport of secretory proteins in Drosophila.
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http://dx.doi.org/10.1083/jcb.202403016 | DOI Listing |
The p24-family member, TMED9, has recently emerged as a player in secretory pathway protein quality control (PQC) that influences the trafficking and degradation of misfolded proteins. Here we show that TMED9 plays a central role in the PQC of GPI-anchored proteins (GPI-APs). Typically, upon release from the endoplasmic reticulum (ER)-resident chaperone calnexin, misfolded GPI-APs traffic to the Golgi by an ER-export pathway called Rapid ER stress-induced Export (RESET).
View Article and Find Full Text PDFAm J Hum Genet
March 2025
UCL Institute of Ophthalmology, University College London, London, UK. Electronic address:
In two unrelated families with X-linked inherited retinal dystrophy, identification of the causative variants was elusive. Interrogation of the next-generation sequencing (NGS) data revealed a "dark" intergenic region on Xq27.1 with poor coverage.
View Article and Find Full Text PDFInt J Biol Macromol
March 2025
Key Laboratory of National Forestry and Grassland Administration on Biodiversity Conservation in Karst Mountainous Areas of Southwestern China, School of Life Sciences, Guizhou Normal University, Guiyang 550025, China. Electronic address:
ER stress activates the unfolded protein response (UPR), a critical mechanism for maintaining cellular homeostasis in plants. The p24 protein family is known to be involved in protein trafficking between the endoplasmic reticulum (ER) and the Golgi apparatus, but its role in ER stress remains unclear in plants. In this study, we found that Atp24δ8(delta8), a member of the δ-2 subclass of the p24 family, is significantly upregulated in response to tunicamycin-induced ER stress.
View Article and Find Full Text PDFTransl Cancer Res
October 2024
College of Biotechnology, Tianjin University of Science and Technology, Tianjin, China.
Background: Transmembrane p24 trafficking protein 9 () belongs to the TMED family, and its overexpression frequently induces cancer. Studies have demonstrated the association between the overexpression of and cancer development and proliferative migration in cancers such as ovarian cancer, hepatocellular carcinoma, and breast cancer. However, there has been no study investigating the clinical value, biological function, and anti-tumor immune effects of from a pan-cancer perspective.
View Article and Find Full Text PDFJ Immunother Cancer
November 2024
Department of Molecular oncology and immunology, Netherlands Cancer Institute, Oncode Institute, Amsterdam, The Netherlands
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