Loss of the novel Vcp (valosin containing protein) interactor Washc4 interferes with autophagy-mediated proteostasis in striated muscle and leads to myopathy in vivo
Open accessAbstract
VCP/p97 (valosin containing protein) is a key regulator of cellular proteostasis. It orchestrates protein turnover and quality control in vivo, processes fundamental for proper cell function. In humans, mutations in VCP lead to severe myo- and neuro-degenerative disorders such as inclusion body myopathy with Paget disease of the bone and frontotemporal dementia (IBMPFD), amyotrophic lateral sclerosis (ALS) or and hereditary spastic paraplegia (HSP). We analyzed here the in vivo role of Vcp and its novel interactor Washc4/Swip (WASH complex subunit 4) in the vertebrate model zebrafish (Danio rerio). We found that targeted inactivation of either Vcp or Washc4, led to progressive impairment of cardiac and skeletal muscle function, structure and cytoarchitecture without interfering with the differentiation of both organ systems. Notably, loss of Vcp resulted in compromised protein degradation via the proteasome and the macroautophagy/autophagy machinery, whereas Washc4 deficiency did not affect the function of the ubiquitin-proteasome system (UPS) but caused ER stress and interfered with autophagy function in vivo. In summary, our findings provide novel insights into the in vivo functions of Vcp and its novel interactor Washc4 and their particular and distinct roles during proteostasis in striated muscle cells.
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p97/VCP deficiency results in accumulation of numerous vesicular bodies, autophagy impairment, and altered myofibrillar organization, causing a severe myopathy.
“Moreover, p97/VCP deficiency resulted in the accumulation of numerous vesicular bodies, autophagy impairment, and altered myofibrillar organization, causing a severe myopathy.”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [175]
Inhibition of p97/VCP in zebrafish leads to mitochondrial morphology and cristae alterations in skeletal muscle and the heart.
“Similarly, the inhibition of p97/VCP in zebrafish leads to mitochondrial morphology and cristae alterations in skeletal muscle and the heart [175].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [175]
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Self-citationMatthews, I., Birmbaum, A., Gromova, A., Coutinho, K., McGraw, M., Patterson, D. C., Banks, M. T., Nobles, A. C., Nguyen, N., Miranda, H. C., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1578234/v1
Nitrogen Mustard Induced Protein Influx in Nucleus and Metabolism Change and p97 Mediated the RepairPreprint
Cheng, J. S., Yu, W., Liu, H., Dong, X., Sai, Y., Ye, F., Dan, G., Chen, M., Zhao, Y., Zhang, X., et al. (2023) · Research Square · doi:10.21203/rs.3.rs-2448806/v1
WASHC3 knockout disrupts mitochondrial protein homeostasis and energy metabolism in cardiomyocytes
Kim, S. Y., Park, D.-D., Glazier, A. A., Rottbauer, W., & Just, S. (2026) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2026.1682381
Self-citationSmarca4 maintains mitochondrial homeostasis and energy metabolism during cardiac development
Park, D.-D., Kim, S. Y., Boos, A., Andrasch, Y., Krieg, L., Rottbauer, W., & Just, S. (2026) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-026-06168-3
Self-citationCheng, J., Yang, Y., Liu, H., Sai, Y., Zou, X., & Zhou, W. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.116643
Diofano, F., Allhoff, B., Park, D.-D., Hartmann, L., Rottbauer, W., & Just, S. (2026) · Molecular and Cellular Biology · doi:10.1080/10985549.2026.2664584
Self-citation
- Authors
- Kustermann, M., Manta, L., Paone, C., Kustermann, J., Lausser, L., Wiesner, C., Eichinger, L., Clemen, C. S., Schröder, R., Kestler, H. A., Sandri, M., Rottbauer, W., & Just, S.
- Affiliations
- Universität Ulm (DE)
- University of Cologne (DE)
- Universitätsklinikum Erlangen (DE)
- University of Padua (IT)
- Corresponding author
- Just, Steffen
- ORCID
- Venue
- Autophagy
- Publisher
- Informa UK Limited
- Published
- 2018-08-16
- Volume
- 14
- Issue
- 11
- Pages
- 1911-1927
- ISSN
- 1554-8627 (ISSN-L)
- 1554-8635
- PMC
- PMC6152520
- OpenAlex
- W2884593672
- Cited by
- 45
- References
- 50
- Citations by year
- 2026: 4 · 2024: 6 · 2023: 7 · 2022: 10 · 2021: 8 · 2020: 5 · 2019: 3 · 2018: 2
- FWCI
- 3.51
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Autophagy (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Kölner Universitäts PublikationsServer (Universität zu Köln) (publishedVersion)
- Padua Research Archive (University of Padova) (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft (RO217¾-1 (WR), RO217¾-2 (WR), JU2859/1–2 (SJ))
- Ministerium Wissenschaft, Forschung und Kunst Baden-Württemberg (Juniorprofessurenprogramm 2013)
- German Federal Ministry of Education and Research (e:Med-SYMBOL-HF grant #01ZX1407A)
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- VCP/p97, WASH complex, proteostasis, striated muscle, myopathy, zebrafish, myocardium, skeletal muscle, protein degradation, proteasome, endoplasmic reticulum stress, ubiquitin-proteasome system, hereditary spastic paraplegia, amyotrophic lateral sclerosis
- MeSH terms
- Valosin Containing Protein, Proteostasis, Animals, Autophagy, Embryo, Nonmammalian, Humans, Male, Muscular Diseases, Protein Binding, Zebrafish, Gene Deletion, Muscle, Skeletal, Zebrafish Proteins, Animals, Genetically Modified, Intracellular Signaling Peptides and Proteins, Mice, Muscle, Striated, HEK293 Cells
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