ArticleThe Journal of biological chemistry2019
The chaperone ERp29 is required for tunneling nanotube formation by stabilizing MSec.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 49 citations in OpenAlex.
- Building the bridges: molecular mechanisms of tunneling nanotube formation.Cellular and molecular life sciences : CMLS · 2026Review
- Breaking cellular boundaries: molecular mechanisms of tunneling nanotube formation and fusion.Biochemical Society transactions · 2026Review
- Mobile Powerhouses: Mitochondria Transfer via Tunnelling Nanotubes in Brain Health and Neurodegenerative Diseases.The European journal of neuroscience · 2026Review
- CD13 activation assembles phosphoinositide (PI) signaling complexes to regulate the actin cytoskeleton.Scientific reports · 2026Article
- Mitochondrial abnormalities in nondiabetic and nonhypertensive glomerular diseases: a comprehensive review.Molecular and cellular biochemistry · 2026Review
- Bone marrow mesenchymal stem cells transport connexin43 via tunneling nanotubes to alleviate isopreterenol-induced myocardial hypertrophy.Stem cell research & therapy · 2025Article
- Identification of TNFAIP2 as a unique cellular regulator of CSF-1 receptor activation.Life science alliance · 2025Article
- M-Sec promotes the accumulation of intracellular HTLV-1 Gag puncta and the incorporation of Env into viral particles.PLoS pathogens · 2025Article
- A novel process for transcellular hemoglobin transport from macrophages to cancer cells.Cell communication and signaling : CCS · 2024Article
- Potential Mechanisms of Tunneling Nanotube Formation and Their Role in Pathology Spread in Alzheimer's Disease and Other Proteinopathies.International journal of molecular sciences · 2024Review
- Proteomic landscape of tunneling nanotubes reveals CD9 and CD81 tetraspanins as key regulators.eLife · 2024Article
- A role for tunneling nanotubes in virus spread.Frontiers in microbiology · 2024Review
- Intercellular Highways in Transport Processes.Results and problems in cell differentiation · 2024Review
- Highly Specialized Mechanisms for Mitochondrial Transport in Neurons: From Intracellular Mobility to Intercellular Transfer of Mitochondria.Biomolecules · 2023Review
- Article
- The role of tumor neogenesis pipelines in tumor progression and their therapeutic potential.Cancer medicine · 2023Review
- Review
- Tunneling Nanotubes: A New Target for Nanomedicine?International journal of molecular sciences · 2022Review
- M-Sec induced by HTLV-1 mediates an efficient viral transmission.PLoS pathogens · 2021Article
- Secretome and Tunneling Nanotubes: A Multilevel Network for Long Range Intercellular Communication between Endothelial Cells and Distant Cells.International journal of molecular sciences · 2021Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tunneling nanotubes (TNTs) are membrane conduits that mediate long-distance intercellular cross-talk in several organisms and play vital roles during development, pathogenic transmission, and cancer metastasis. However, the molecular mechanisms of TNT formation and function remain poorly understood. The protein MSec (also known as TNFα-induced protein 2 (TNFAIP2) and B94) is essential for TNT formation in multiple cell types. Here, using affinity protein purification, mass spectrometric identification, and confocal immunofluorescence microscopy assays, we found that MSec interacts with the endoplasmic reticulum (ER) chaperone ERp29. siRNA-mediated ERp29 depletion in mammalian cells significantly reduces TNT formation, whereas its overexpression induces TNT formation, but in a strictly MSec-dependent manner. ERp29 stabilized MSec protein levels, but not its mRNA levels, and the chaperone activity of ERp29 was required for maintaining MSec protein stability. Subcellular ER fractionation and subsequent limited proteolytic treatment suggested that MSec is associated with the outer surface of the ER. The ERp29-MSec interaction appeared to require the presence of other bridging protein(s), perhaps triggered by post-translational modification of ERp29. Our study implicates MSec as a target of ERp29 and reveals an indispensable role for the ER in TNT formation, suggesting new modalities for regulating TNT numbers in cells and tissues.
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