Previously we showed that membrane fusion is required for TANGO1-dependent export of procollagen VII from the endoplasmic reticulum (ER) (Nogueira, et al., 2014). Along with the t-SNARE Syntaxin 18, we now reveal the complete complement of SNAREs required in this process, t-SNAREs BNIP1 and USE1, and v-SNARE YKT6. TANGO1 recruits YKT6-containing ER Golgi Intermediate Compartment (ERGIC) membranes to procollagen VII-enriched patches on the ER. Moreover residues 1214-1396, that include the first coiled coil of TANGO1, specifically recruit ERGIC membranes even when targeted to mitochondria. TANGO1 is thus pivotal in concentrating procollagen VII in the lumen and recruiting ERGIC membranes on the cytoplasmic surface of the ER. Our data reveal that growth of a mega transport carrier for collagen export from the ER is not by acquisition of a larger patch of ER membrane, but instead by addition of ERGIC membranes to procollagen-enriched domains of the ER by a TANGO1-mediated process.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4709264PMC
http://dx.doi.org/10.7554/eLife.10982DOI Listing

Publication Analysis

Top Keywords

ergic membranes
20
tango1 recruits
8
endoplasmic reticulum
8
procollagen vii
8
ergic
5
membranes
5
tango1
4
recruits ergic
4
membranes endoplasmic
4
procollagen
4

Similar Publications

The present study explores the conformational dynamics of the membrane protein of Middle East Respiratory Syndrome Coronavirus (MERS-CoV) within the Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC) complex using an all-atomistic molecular dynamics simulation approach. Significant structural changes were observed in the N-terminal, C-terminal, transmembrane, and beta-sheet sandwich domains of the MERS-CoV membrane protein. This study also highlights the structural similarities between the MERS-CoV and the SARS-CoV-2 membrane proteins, particularly in how both exhibit a distinct kink in the transmembrane helix caused by aromatic residue-lipid interactions.

View Article and Find Full Text PDF
Article Synopsis
  • - The study investigates how SARS-CoV-2 buds and transports its virions from the ERGIC to the cell surface, revealing that the vesicles involved have a protein coat known as coatomer complex I (COPI).
  • - Researchers observed that during infection, the distribution of COPI and the ERGIC changed, suggesting they play a role in the virus's replication process.
  • - Depleting a key COPI component, COPB2, confined the SARS-CoV-2 virions within the ERGIC and significantly reduced viral release, indicating that targeting COPI could be a potential strategy for developing antiviral treatments.
View Article and Find Full Text PDF
Article Synopsis
  • - Mitochondrial dysfunction and oxidative stress are significant factors in age-related neurodegenerative diseases, and PKCδ isoform in dopaminergic neurons is critical for cell death during these stress events through caspase-3 activation.
  • - The study revealed that upon mitochondrial dysfunction, PKCδ gets activated and moves to the nucleus, where it interacts with Lamin B1, causing nuclear damage and contributing to neuronal cell death.
  • - Experiments showed that blocking PKCδ activation or modifying Lamin B1 can prevent nuclear damage, confirming PKCδ's role as a major player in neurodegenerative processes linked to mitochondrial stress.
View Article and Find Full Text PDF

The precise cellular mechanisms underlying heightened proinflammatory cytokine production during coronavirus infection remain incompletely understood. Here we identify the envelope (E) protein in severe coronaviruses (SARS-CoV-2, SARS, or MERS) as a potent inducer of interleukin-1 release, intensifying lung inflammation through the activation of TMED10-mediated unconventional protein secretion (UcPS). In contrast, the E protein of mild coronaviruses (229E, HKU1, or OC43) demonstrates a less pronounced effect.

View Article and Find Full Text PDF

The chromodomain protein CDYL confers forebrain identity to human cortical organoids by inhibiting neuronatin.

Cell Rep

October 2024

Neuroscience Research Institute and Department of Neurobiology, School of Basic Medical Sciences, Key Laboratory for Neuroscience, Ministry of Education/National Health Commission and State Key Laboratory of Natural and Biomimetic Drugs, Peking University, Beijing 100191, China; PKU-IDG/McGovern Institute for Brain Research, Peking University, Beijing 100871, China. Electronic address:

Fate determination of neural stem cells (NSCs) is crucial for cortex development and is closely linked to neurodevelopmental disorders when gene expression networks are disrupted. The transcriptional corepressor chromodomain Y-like (CDYL) is widely expressed across diverse cell populations within the human embryonic cortex. However, its precise role in cortical development remains unclear.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!