CoChat
Sign Up
Cited by 123

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Dual Cleavage of Neuregulin 1 Type III by BACE1 and ADAM17 Liberates Its EGF-Like Domain and Allows Paracrine Signaling

Fleck, Daniel, van Bebber, Frauke, Colombo, Alessio, Galante, Chiara, Schwenk, Benjamin M., Rabe, Linnea, Hampel, Heike, Novak, Bozidar, Kremmer, Elisabeth, Tahirovic, Sabina, Edbauer, Dieter, Lichtenthaler, Stefan F., Schmid, Bettina, Willem, Michael, Haass, Christian·2013·The Journal of Neuroscience
DOI 10.1523/jneurosci.3372-12.2013
Open this paper in CoChat — free account

Abstract

Proteolytic shedding of cell surface proteins generates paracrine signals involved in numerous signaling pathways. Neuregulin 1 (NRG1) type III is involved in myelination of the peripheral nervous system, for which it requires proteolytic activation by proteases of the ADAM family and BACE1. These proteases are major therapeutic targets for the prevention of Alzheimer's disease because they are also involved in the proteolytic generation of the neurotoxic amyloid β-peptide. Identification and functional investigation of their physiological substrates is therefore of greatest importance in preventing unwanted side effects. Here we investigated proteolytic processing of NRG1 type III and demonstrate that the ectodomain can be cleaved by three different sheddases, namely ADAM10, ADAM17, and BACE1. Surprisingly, we not only found cleavage by ADAM10, ADAM17, and BACE1 C-terminal to the epidermal growth factor (EGF)-like domain, which is believed to play a pivotal role in signaling, but also additional cleavage sites for ADAM17 and BACE1 N-terminal to that domain. Proteolytic processing at N- and C-terminal sites of the EGF-like domain results in the secretion of this domain from NRG1 type III. The soluble EGF-like domain is functionally active and stimulates ErbB3 signaling in tissue culture assays. Moreover, the soluble EGF-like domain is capable of rescuing hypomyelination in a zebrafish mutant lacking BACE1. Our data suggest that NRG1 type III-dependent myelination is not only controlled by membrane-retained NRG1 type III, but also in a paracrine manner via proteolytic liberation of the EGF-like domain.

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1523/jneurosci.3372-12.2013

Cites

5 of 5 references verified0 citation errors · 0 not checkable

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.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • BACE1 is highly expressed in the nervous system and contributes to additional physiological processes besides its role in AD, e.g., through neuregulin-1 cleavage in myelination and CHL1 cleavage in axon targeting.

    “BACE1 is highly expressed in the nervous system and contributes to additional physiological processes besides its role in AD, e.g. through neuregulin-1 cleavage in myelination and CHL1 cleavage in axon targeting [7–12].”

    From Seizure protein 6 and its homolog seizure 6-like protein are physiological substrates of BACE1 in neurons (2016) · cites this paper as [9]

    The Introduction says BACE1 processes neuregulin-1 type III, a regulator of peripheral nervous system myelination, and the Discussion reports that a BACE1-liberated neuregulin domain promotes myelination in zebrafish. The passages do not support the sentence’s separate claims that BACE1 is highly expressed in the nervous system or that CHL1 cleavage contributes to axon targeting. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • BACE1 cleavage of NRG1 regulates myelination.

    “BACE1 cleavage of NRG1 regulates myelination,”

    From BACE1: More than just a β‐secretase (2022) · cites this paper as [26]

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

Flagged first, then by citations

Research works printed but not linked: 46

  1. 10.1083/jcb.200212085 · DOI
  2. 10.1038/nn1342 · DOI
  3. 10.1002/glia.20753 · DOI
  4. 10.1016/j.yexcr.2008.10.011 · DOI
  5. 10.1016/j.neuron.2008.06.028 · DOI
  6. 10.1016/S0092-8674(00)80675-3 · DOI · Paper page
  7. 10.1042/BJ20090549 · DOI
  8. 10.1074/jbc.M003202200 · DOI · Paper page
  9. 10.1523/JNEUROSCI.0605-10.2010 · DOI
  10. 10.1016/0896-6273(95)90323-2 · DOI
  11. 10.1038/nrneurol.2009.218 · DOI · Paper page
  12. 10.1186/1559-0275-8-9 · DOI
  13. 10.1083/jcb.139.6.1495 · DOI · Paper page
  14. 10.1023/B:NEUR.0000020614.83883.be · DOI
  15. 10.1038/sj.emboj.7600061 · DOI
  16. 10.1016/j.ydbio.2005.05.004 · DOI
  17. 10.1038/nn1797 · DOI · Paper page
  18. 10.1096/fj.08-106666 · DOI · Paper page
  19. Karey, 1988, Differential responsiveness of human breast cancer cell lines MCF-7 and T47D to growth factors and 17 beta-estradiol, Cancer Res, 48, 4083
  20. 10.1002/aja.1002030302 · DOI · Paper page
  21. 10.1016/0092-8674(86)90841-X · DOI
  22. 10.1152/physiol.00028.2010 · DOI
  23. 10.1038/nn.2849 · DOI
  24. 10.1111/j.1471-4159.2011.07248.x · DOI · Paper page
  25. 10.2174/1386207053258488 · DOI
  26. 10.1074/jbc.M111.251538 · DOI
  27. 10.1126/science.1095862 · DOI
  28. 10.1016/j.conb.2009.08.006 · DOI
  29. 10.1006/mcne.2000.0896 · DOI
  30. 10.1002/glia.21260 · DOI
  31. 10.1016/j.semcdb.2010.08.008 · DOI
  32. 10.1093/emboj/cdf541 · DOI
  33. 10.1038/embor.2012.90 · DOI
  34. 10.1242/dev.068072 · DOI
  35. 10.1080/08977190600634373 · DOI
  36. 10.1093/embo-reports/kve180 · DOI
  37. 10.1074/jbc.M007913200 · DOI
  38. 10.1523/JNEUROSCI.1681-09.2010 · DOI
  39. 10.1016/j.neuron.2005.08.017 · DOI
  40. 10.1038/emboj.2012.42 · DOI
  41. 10.1111/jnc.12198 · DOI
  42. 10.1186/alzrt82 · DOI
  43. 10.1002/glia.21255 · DOI
  44. 10.1074/jbc.M005700200 · DOI
  45. 10.1074/jbc.M601542200 · DOI
  46. 10.1016/S0896-6273(00)80873-9 · DOI

Cited by

Sorted by citations

Metadata

Authors
Fleck, D., van Bebber, F., Colombo, A., Galante, C., Schwenk, B. M., Rabe, L., Hampel, H., Novak, B., Kremmer, E., Tahirovic, S., Edbauer, D., Lichtenthaler, S. F., Schmid, B., Willem, M., & Haass, C.
Venue
The Journal of Neuroscience
Publisher
Society for Neuroscience
Published
2013-05-01
Volume
33
Issue
18
Pages
7856-7869
ISSN
  • 0270-6474
  • 1529-2401
DOI
10.1523/jneurosci.3372-12.2013
Cited by
123
References
5
Language
en
Licence
creativecommons.org/licenses/by-nc-sa/4.0/ (vor, 184 d)

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