Cargando…
Effect of the protease plasmin on C. elegans hyperactive DEG/ENaC channels MEC-4(d) and UNC-8(d)
C. elegans MEC-4 and UNC-8 belong to the DEG/ENaC family of voltage-independent Na(+) channels and have been implicated in mechanosensation and synaptic remodeling. MEC-4 and UNC-8 hyperactive mutants, designated (d) mutants, conduct enhanced currents and cause cell death due to uncontrolled influx...
Autores principales: | , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Caltech Library
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8223032/ https://www.ncbi.nlm.nih.gov/pubmed/34189421 http://dx.doi.org/10.17912/micropub.biology.000412 |
_version_ | 1783711610527809536 |
---|---|
author | Johnson, Christina K. Miller, David D. Bianchi, Laura |
author_facet | Johnson, Christina K. Miller, David D. Bianchi, Laura |
author_sort | Johnson, Christina K. |
collection | PubMed |
description | C. elegans MEC-4 and UNC-8 belong to the DEG/ENaC family of voltage-independent Na(+) channels and have been implicated in mechanosensation and synaptic remodeling. MEC-4 and UNC-8 hyperactive mutants, designated (d) mutants, conduct enhanced currents and cause cell death due to uncontrolled influx of cations. We show here that MEC-4(d) but not UNC-8(d) currents are further potentiated by treatment with the protease plasmin and that this effect is dependent upon co-expression with the chaperon protein MEC-6. Mammalian DEG/ENaC channels are cleaved by plasmin in the channel finger domain and both MEC-4 and UNC-8 have a predicted plasmin cleavage site in this domain. We previously showed that MEC-4(d), but not UNC-8(d), currents are increased by co-expression with MEC-6, which interacts with the channel via the finger domain. We suggest that interaction of the channel subunit with MEC-6 may render the plasmin cleavage site more accessible. Given that C. elegans expresses a homolog of plasmin, these effects might be relevant in vivo. |
format | Online Article Text |
id | pubmed-8223032 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Caltech Library |
record_format | MEDLINE/PubMed |
spelling | pubmed-82230322021-06-28 Effect of the protease plasmin on C. elegans hyperactive DEG/ENaC channels MEC-4(d) and UNC-8(d) Johnson, Christina K. Miller, David D. Bianchi, Laura MicroPubl Biol New Finding C. elegans MEC-4 and UNC-8 belong to the DEG/ENaC family of voltage-independent Na(+) channels and have been implicated in mechanosensation and synaptic remodeling. MEC-4 and UNC-8 hyperactive mutants, designated (d) mutants, conduct enhanced currents and cause cell death due to uncontrolled influx of cations. We show here that MEC-4(d) but not UNC-8(d) currents are further potentiated by treatment with the protease plasmin and that this effect is dependent upon co-expression with the chaperon protein MEC-6. Mammalian DEG/ENaC channels are cleaved by plasmin in the channel finger domain and both MEC-4 and UNC-8 have a predicted plasmin cleavage site in this domain. We previously showed that MEC-4(d), but not UNC-8(d), currents are increased by co-expression with MEC-6, which interacts with the channel via the finger domain. We suggest that interaction of the channel subunit with MEC-6 may render the plasmin cleavage site more accessible. Given that C. elegans expresses a homolog of plasmin, these effects might be relevant in vivo. Caltech Library 2021-06-21 /pmc/articles/PMC8223032/ /pubmed/34189421 http://dx.doi.org/10.17912/micropub.biology.000412 Text en Copyright: © 2021 by the authors https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | New Finding Johnson, Christina K. Miller, David D. Bianchi, Laura Effect of the protease plasmin on C. elegans hyperactive DEG/ENaC channels MEC-4(d) and UNC-8(d) |
title | Effect of the protease plasmin on C. elegans hyperactive DEG/ENaC channels MEC-4(d) and UNC-8(d) |
title_full | Effect of the protease plasmin on C. elegans hyperactive DEG/ENaC channels MEC-4(d) and UNC-8(d) |
title_fullStr | Effect of the protease plasmin on C. elegans hyperactive DEG/ENaC channels MEC-4(d) and UNC-8(d) |
title_full_unstemmed | Effect of the protease plasmin on C. elegans hyperactive DEG/ENaC channels MEC-4(d) and UNC-8(d) |
title_short | Effect of the protease plasmin on C. elegans hyperactive DEG/ENaC channels MEC-4(d) and UNC-8(d) |
title_sort | effect of the protease plasmin on c. elegans hyperactive deg/enac channels mec-4(d) and unc-8(d) |
topic | New Finding |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8223032/ https://www.ncbi.nlm.nih.gov/pubmed/34189421 http://dx.doi.org/10.17912/micropub.biology.000412 |
work_keys_str_mv | AT johnsonchristinak effectoftheproteaseplasminonceleganshyperactivedegenacchannelsmec4dandunc8d AT millerdavidd effectoftheproteaseplasminonceleganshyperactivedegenacchannelsmec4dandunc8d AT bianchilaura effectoftheproteaseplasminonceleganshyperactivedegenacchannelsmec4dandunc8d |