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Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation
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| Zeitschriftentitel: | Bioscience Reports |
|---|---|
| Personen und Körperschaften: | |
| In: | Bioscience Reports, 33, 2013, 3 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Portland Press Ltd.
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| Schlagwörter: |
| author_facet |
Katafuchi, Takeshi Katafuchi, Takeshi |
|---|---|
| author |
Katafuchi, Takeshi |
| spellingShingle |
Katafuchi, Takeshi Bioscience Reports Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation Cell Biology Molecular Biology Biochemistry Biophysics |
| author_sort |
katafuchi, takeshi |
| spelling |
Katafuchi, Takeshi 0144-8463 1573-4935 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry Biophysics http://dx.doi.org/10.1042/bsr20130025 <jats:p>In this study, Tyr808 in GC-B (guanylate cyclase-B), a receptor of the CNP (C-type natriuretic peptide), has been shown to be a critical regulator of GC-B activity. In searching for phosphorylation sites that could account for suppression of GC-B activity by S1P (sphingosine-1-phosphate), mutations were introduced into several candidate serine/threonine and tyrosine residues. Although no novel phosphorylation sites that influenced the suppression of GC-B were identified, experiments revealed that mutations in Tyr808 markedly enhanced GC-B activity. CNP-stimulated activities of the Y808F and Y808A mutants were greater than 30-fold and 70-fold higher, respectively, than that of WT (wild-type) GC-B. The Y808E and Y808S mutants were constitutively active, expressing 270-fold higher activity without CNP stimulation than WT GC-B. Those mutations also influenced the sensitivity of GC-B to a variety of inhibitors, including S1P, Na3VO4 and PMA. Y808A, Y808E and Y808S mutations markedly weakened S1P- and Na3VO4-dependent suppression of GC-B activity, whereas Y808E and Y808S mutations rather elevated cGMP production. Tyr808 is conserved in all membrane-bound GCs and located in the niche domain showing sequence similarity to a partial fragment of the HNOBA (haem nitric oxide binding associated) domain, which is found in soluble GC and in bacterial haem-binding kinases. This finding provides new insight into the activation mechanism of GCs.</jats:p> Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation Bioscience Reports |
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| title |
Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation |
| title_unstemmed |
Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation |
| title_full |
Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation |
| title_fullStr |
Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation |
| title_full_unstemmed |
Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation |
| title_short |
Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation |
| title_sort |
mutations in tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-b regulation |
| topic |
Cell Biology Molecular Biology Biochemistry Biophysics |
| url |
http://dx.doi.org/10.1042/bsr20130025 |
| publishDate |
2013 |
| physical |
|
| description |
<jats:p>In this study, Tyr808 in GC-B (guanylate cyclase-B), a receptor of the CNP (C-type natriuretic peptide), has been shown to be a critical regulator of GC-B activity. In searching for phosphorylation sites that could account for suppression of GC-B activity by S1P (sphingosine-1-phosphate), mutations were introduced into several candidate serine/threonine and tyrosine residues. Although no novel phosphorylation sites that influenced the suppression of GC-B were identified, experiments revealed that mutations in Tyr808 markedly enhanced GC-B activity. CNP-stimulated activities of the Y808F and Y808A mutants were greater than 30-fold and 70-fold higher, respectively, than that of WT (wild-type) GC-B. The Y808E and Y808S mutants were constitutively active, expressing 270-fold higher activity without CNP stimulation than WT GC-B. Those mutations also influenced the sensitivity of GC-B to a variety of inhibitors, including S1P, Na3VO4 and PMA. Y808A, Y808E and Y808S mutations markedly weakened S1P- and Na3VO4-dependent suppression of GC-B activity, whereas Y808E and Y808S mutations rather elevated cGMP production. Tyr808 is conserved in all membrane-bound GCs and located in the niche domain showing sequence similarity to a partial fragment of the HNOBA (haem nitric oxide binding associated) domain, which is found in soluble GC and in bacterial haem-binding kinases. This finding provides new insight into the activation mechanism of GCs.</jats:p> |
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| description | <jats:p>In this study, Tyr808 in GC-B (guanylate cyclase-B), a receptor of the CNP (C-type natriuretic peptide), has been shown to be a critical regulator of GC-B activity. In searching for phosphorylation sites that could account for suppression of GC-B activity by S1P (sphingosine-1-phosphate), mutations were introduced into several candidate serine/threonine and tyrosine residues. Although no novel phosphorylation sites that influenced the suppression of GC-B were identified, experiments revealed that mutations in Tyr808 markedly enhanced GC-B activity. CNP-stimulated activities of the Y808F and Y808A mutants were greater than 30-fold and 70-fold higher, respectively, than that of WT (wild-type) GC-B. The Y808E and Y808S mutants were constitutively active, expressing 270-fold higher activity without CNP stimulation than WT GC-B. Those mutations also influenced the sensitivity of GC-B to a variety of inhibitors, including S1P, Na3VO4 and PMA. Y808A, Y808E and Y808S mutations markedly weakened S1P- and Na3VO4-dependent suppression of GC-B activity, whereas Y808E and Y808S mutations rather elevated cGMP production. Tyr808 is conserved in all membrane-bound GCs and located in the niche domain showing sequence similarity to a partial fragment of the HNOBA (haem nitric oxide binding associated) domain, which is found in soluble GC and in bacterial haem-binding kinases. This finding provides new insight into the activation mechanism of GCs.</jats:p> |
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| spelling | Katafuchi, Takeshi 0144-8463 1573-4935 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry Biophysics http://dx.doi.org/10.1042/bsr20130025 <jats:p>In this study, Tyr808 in GC-B (guanylate cyclase-B), a receptor of the CNP (C-type natriuretic peptide), has been shown to be a critical regulator of GC-B activity. In searching for phosphorylation sites that could account for suppression of GC-B activity by S1P (sphingosine-1-phosphate), mutations were introduced into several candidate serine/threonine and tyrosine residues. Although no novel phosphorylation sites that influenced the suppression of GC-B were identified, experiments revealed that mutations in Tyr808 markedly enhanced GC-B activity. CNP-stimulated activities of the Y808F and Y808A mutants were greater than 30-fold and 70-fold higher, respectively, than that of WT (wild-type) GC-B. The Y808E and Y808S mutants were constitutively active, expressing 270-fold higher activity without CNP stimulation than WT GC-B. Those mutations also influenced the sensitivity of GC-B to a variety of inhibitors, including S1P, Na3VO4 and PMA. Y808A, Y808E and Y808S mutations markedly weakened S1P- and Na3VO4-dependent suppression of GC-B activity, whereas Y808E and Y808S mutations rather elevated cGMP production. Tyr808 is conserved in all membrane-bound GCs and located in the niche domain showing sequence similarity to a partial fragment of the HNOBA (haem nitric oxide binding associated) domain, which is found in soluble GC and in bacterial haem-binding kinases. This finding provides new insight into the activation mechanism of GCs.</jats:p> Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation Bioscience Reports |
| spellingShingle | Katafuchi, Takeshi, Bioscience Reports, Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation, Cell Biology, Molecular Biology, Biochemistry, Biophysics |
| title | Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation |
| title_full | Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation |
| title_fullStr | Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation |
| title_full_unstemmed | Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation |
| title_short | Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation |
| title_sort | mutations in tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-b regulation |
| title_unstemmed | Mutations in Tyr808 reveal a potential auto-inhibitory mechanism of guanylate cyclase-B regulation |
| topic | Cell Biology, Molecular Biology, Biochemistry, Biophysics |
| url | http://dx.doi.org/10.1042/bsr20130025 |