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CA10 regulates neur...
CA10 regulates neurexin heparan sulfate addition via a direct binding in the secretory pathway
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- Montoliu-Gaya, Laia (författare)
- Gothenburg University,Göteborgs universitet,Wallenberg Centre for Molecular and Translational Medicine,Institutionen för biomedicin,Institute of Biomedicine
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- Tietze, Daniel, 1980 (författare)
- Gothenburg University,Göteborgs universitet,Wallenberg Centre for Molecular and Translational Medicine,Institutionen för kemi och molekylärbiologi,Department of Chemistry and Molecular Biology
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- Kaminski, Debora (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för biomedicin,Wallenberg Centre for Molecular and Translational Medicine,Institute of Biomedicine
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Mirgorodskaya, E. (författare)
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- Tietze, Alesia A., 1984 (författare)
- Gothenburg University,Göteborgs universitet,Institutionen för kemi och molekylärbiologi,Wallenberg Centre for Molecular and Translational Medicine,Department of Chemistry and Molecular Biology
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- Sterky, Fredrik H (författare)
- Gothenburg University,Göteborgs universitet,Wallenberg Centre for Molecular and Translational Medicine,Institutionen för biomedicin,Institute of Biomedicine
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(creator_code:org_t)
- 2021-02-15
- 2021
- Engelska.
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Ingår i: Embo Reports. - : EMBO. - 1469-221X .- 1469-3178. ; 22:4
- Relaterad länk:
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https://doi.org/10.1...
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https://gup.ub.gu.se...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Neurexins are presynaptic adhesion molecules that shape the molecular composition of synapses. Diversification of neurexins in numerous isoforms is believed to confer synapse-specific properties by engaging with distinct ligands. For example, a subset of neurexin molecules carry a heparan sulfate (HS) glycosaminoglycan that controls ligand binding, but how this post-translational modification is controlled is not known. Here, we observe that CA10, a ligand to neurexin in the secretory pathway, regulates neurexin-HS formation. CA10 is exclusively found on non-HS neurexin and CA10 expressed in neurons is sufficient to suppress HS addition and attenuate ligand binding and synapse formation induced by ligands known to recruit HS. This effect is mediated by a direct interaction in the secretory pathway that blocks the primary step of HS biosynthesis: xylosylation of the serine residue. NMR reveals that CA10 engages residues on either side of the serine that can be HS-modified, suggesting that CA10 sterically blocks xylosyltransferase access in Golgi. These results suggest a mechanism for the regulation of HS on neurexins and exemplify a new mechanism to regulate site-specific glycosylations.
Ämnesord
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
Nyckelord
- CA10
- carbonic anhydrase‐
- related protein
- heparan sulfate
- neurexin
- synapse
- Biochemistry & Molecular Biology
- Cell Biology
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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