The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Actin Filament Turnover Drives Leading Edge Growth during Myelin Sheath Formation in the Central Nervous System
Open accessAbstract
Summary During central nervous system development, oligodendrocytes wrap their plasma membrane around axons to generate multi-lamellar myelin sheaths. To drive growth at the leading edge of myelin at the interface with the axon, mechanical forces are necessary, but the underlying mechanisms are not known. Using an interdisciplinary approach that combines morphological, genetic and biophysical analyses, we identified a key role for actin filament network turnover in myelin growth. At the onset of myelin biogenesis, F-actin is redistributed to the leading edge, where its polymerization-based forces push out non-adhesive and motile protrusions. F-actin disassembly converts protrusions into sheets by reducing surface tension and in turn inducing membrane spreading and adhesion. We identified the actin depolymerizing factor ADF/Cofilin1, which mediates high F-actin turnover rates, as essential factor in this process. We propose that F-actin turnover is the driving force in myelin wrapping by regulating repetitive cycles of leading edge protrusion and spreading.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Cahoy, J. D., Emery, B., Kaushal, A., Foo, L. C., Zamanian, J. L., Christopherson, K. S., Xing, Y., Lubischer, J. L., Krieg, P. A., Krupenko, S. A., et al. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4178-07.2008 · Cited by 3,129
Rapid leukocyte migration by integrin-independent flowing and squeezing
Lämmermann, T., Bader, B. L., Monkley, S. J., Worbs, T., Wedlich-Söldner, R., Hirsch, K., Keller, M., Förster, R., Critchley, D. R., Fässler, R., et al. (2008) · Nature · doi:10.1038/nature06887 · Cited by 1,397
White matter in learning, cognition, and psychiatric disorders
Fields, R. D. (2008) · Trends in Neurosciences · doi:10.1016/j.tins.2008.04.001 · Cited by 1,337
Disruption of Cnp1 uncouples oligodendroglial functions in axonal support and myelination
Lappe-Siefke, C., Goebbels, S., Gravel, M., Nicksch, E., Lee, J., Braun, P. E., Griffiths, I. R., & Nave, K.-A. (2003) · Nature Genetics · doi:10.1038/ng1095 · Cited by 1,036
ADF/Cofilin: a functional node in cell biology
Bernstein, B. W., & Bamburg, J. R. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2010.01.001 · Cited by 704
Mechanisms of axon ensheathment and myelin growth
Sherman, D. L., & Brophy, P. J. (2005) · Nature Reviews Neuroscience · doi:10.1038/nrn1743 · Cited by 668
Retinoid X receptor gamma signaling accelerates CNS remyelination
Huang, J. K., Jarjour, A. A., Nait Oumesmar, B., Kerninon, C., Williams, A., Krezel, W., Kagechika, H., Bauer, J., Zhao, C., Evercooren, A. B.-V., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2702 · Cited by 547
Synaptic vesicle release regulates myelin sheath number of individual oligodendrocytes in vivo
Mensch, S., Baraban, M., Almeida, R., Czopka, T., Ausborn, J., El Manira, A., & Lyons, D. A. (2015) · Nature Neuroscience · doi:10.1038/nn.3991 · Cited by 398
Self-citationAxin2 as regulatory and therapeutic target in newborn brain injury and remyelination
Fancy, S. P. J., Harrington, E. P., Yuen, T. J., Silbereis, J. C., Zhao, C., Baranzini, S. E., Bruce, C. C., Otero, J. J., Huang, E. J., Nusse, R., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2855 · Cited by 349 · cited 2×
“, 2015) and potential remyelination therapeutics (Fancy et al., 2011; Huang et al., 2011; Deshmukh et al., 2013; Mei et al., 2014) to leading edge activity.”
Dynamics and Mechanisms of CNS Myelination
Bercury, K. K., & Macklin, W. B. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.01.016 · Cited by 320
Cited by
Myelin in the Central Nervous System: Structure, Function, and Pathology
Stadelmann, C., Timmler, S., Barrantes-Freer, A., & Simons, M. (2019) · Physiological Reviews · doi:10.1152/physrev.00031.2018 · Cited by 728
Self-citationMicroglia phagocytose myelin sheaths to modify developmental myelination
Hughes, A. N., & Appel, B. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0654-2 · Cited by 344
Glia in mammalian development and disease
Zuchero, J. B., & Barres, B. A. (2015) · Development · doi:10.1242/dev.129304 · Cited by 304
Autophagy is essential for oligodendrocyte differentiation, survival, and proper myelination
Bankston, A. N., Forston, M. D., Howard, R. M., Andres, K. R., Smith, A. E., Ohri, S. S., Bates, M. L., Bunge, M. B., & Whittemore, S. R. (2019) · Glia · doi:10.1002/glia.23646 · Cited by 112
Mathews, E. S., & Appel, B. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.0726-16.2016 · Cited by 97
Erwig, M. S., Patzig, J., Steyer, A. M., Dibaj, P., Heilmann, M., Heilmann, I., Jung, R. B., Kusch, K., Möbius, W., Jahn, O., et al. (2019) · eLife · doi:10.7554/elife.43888 · Cited by 79
“Since myelin wrapping involves actin disassembly (Nawaz et al., 2015; Zuchero et al., 2015) and myelin compaction requires trafficking of Mbp mRNA along microtubules (Müller et al.”
Galectin-3-Mediated Glial Crosstalk Drives Oligodendrocyte Differentiation and (Re)myelination
Thomas, L., & Pasquini, L. A. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00297 · Cited by 76
Activin receptors regulate the oligodendrocyte lineage in health and disease
Dillenburg, A., Ireland, G., Holloway, R. K., Davies, C. L., Evans, F. L., Swire, M., Bechler, M. E., Soong, D., Yuen, T. J., Su, G. H., et al. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1813-3 · Cited by 75
Silva, A. I., Haddon, J. E., Ahmed Syed, Y., Trent, S., Lin, T.-C. E., Patel, Y., Carter, J., Haan, N., Honey, R. C., Humby, T., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11119-7 · Cited by 71
Oligodendrocyte calcium signaling promotes actin-dependent myelin sheath extension
Iyer, M., Kantarci, H., Cooper, M. H., Ambiel, N., Novak, S. W., Andrade, L. R., Lam, M., Jones, G., Münch, A. E., Yu, X., et al. (2024) · Nature Communications · doi:10.1038/s41467-023-44238-3 · Cited by 49
Leukodystrophy caused by plasmalogen deficiency rescued by glyceryl 1-myristyl ether treatment
Malheiro, A. R., Correia, B., Ferreira da Silva, T., Bessa‐Neto, D., Van Veldhoven, P. P., & Brites, P. (2019) · Brain Pathology · doi:10.1111/bpa.12710 · Cited by 41
Groh, J., Abdelwahab, T., Kattimani, Y., Hörner, M., Loserth, S., Gudi, V., Adalbert, R., Imdahl, F., Saliba, A.-E., Coleman, M., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42570-2 · Cited by 39
Self-citationBoccazzi, M., Macchiarulo, G., Lebon, S., Janowska, J., Le Charpentier, T., Faivre, V., Hua, J., Marangon, D., Lecca, D., Fumagalli, M., et al. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106315 · Cited by 22
Distinct transcriptional changes distinguish efficient and poor remyelination in multiple sclerosis
Chen, J. Q. A., McNamara, N. B., Engelenburg, H. J., Jongejan, A., Wever, D. D., Hopman, K., van Rixel, E., Nijhuis, P. J. H., de Winter, F., Moerland, P. D., et al. (2025) · Brain · doi:10.1093/brain/awae414 · Cited by 17
Identification of genome-wide targets of Olig2 in the adult mouse spinal cord using ChIP-Seq
Darr, A. J., Danzi, M. C., Brady, L., Emig-Agius, D., Hackett, A., Golshani, R., Warner, N., Lee, J., Lemmon, V. P., & Tsoulfas, P. (2017) · PLOS ONE · doi:10.1371/journal.pone.0186091 · Cited by 14
Antagonistic actions of PAK1 and NF2/Merlin drive myelin membrane expansion in oligodendrocytes
Baudouin, L., Adès, N., Kanté, K., Bachelin, C., Hmidan, H., Deboux, C., Panic, R., Ben Messaoud, R., Velut, Y., Hamada, S., et al. (2024) · Glia · doi:10.1002/glia.24570 · Cited by 7
Metadata
- Authors
- Nawaz, S., Sánchez, P., Schmitt, S., Snaidero, N., Mitkovski, M., Velte, C., Brückner, B. R., Alexopoulos, I., Czopka, T., Jung, S. Y., Rhee, J. S., Janshoff, A., Witke, W., Schaap, I. A. T., Lyons, D. A., & Simons, M.
- Venue
- Developmental Cell
- Publisher
- Elsevier BV
- Published
- 2015-07
- Volume
- 34
- Issue
- 2
- Pages
- 139-151
- ISSN
- 1534-5807 (ISSN-L)
- OpenAlex
- W1839988640
- Cited by
- 249
- References
- 11
- FWCI
- 8.47
- Type
- journal article
- Language
- en
- Open access
- bronze
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.