The mechanism of calcium-induced inhibition of muscle fructose 1,6-bisphosphatase and destabilization of glyconeogenic complex.
The mechanism by which calcium inhibits the activity of muscle fructose 1,6-bisphosphatase (FBPase) and destabilizes its interaction with aldolase, regulating glycogen synthesis from non-carbohydrates in skeletal muscle is poorly understood. In the current paper, we demonstrate evidence that Ca(2+)...
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Public Library of Science (PLoS)
2013-01-01
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Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3795747?pdf=render |
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author | Dariusz Rakus Agnieszka Gizak Andrzej A Kasprzak Marek Zarzycki Ewa Maciaszczyk-Dziubinska Andrzej Dzugaj |
author_facet | Dariusz Rakus Agnieszka Gizak Andrzej A Kasprzak Marek Zarzycki Ewa Maciaszczyk-Dziubinska Andrzej Dzugaj |
author_sort | Dariusz Rakus |
collection | DOAJ |
description | The mechanism by which calcium inhibits the activity of muscle fructose 1,6-bisphosphatase (FBPase) and destabilizes its interaction with aldolase, regulating glycogen synthesis from non-carbohydrates in skeletal muscle is poorly understood. In the current paper, we demonstrate evidence that Ca(2+) affects conformation of the catalytic loop 52-72 of muscle FBPase and inhibits its activity by competing with activatory divalent cations, e.g. Mg(2+) and Zn(2+). We also propose the molecular mechanism of Ca(2+)-induced destabilization of the aldolase-FBPase interaction, showing that aldolase associates with FBPase in its active form, i.e. with loop 52-72 in the engaged conformation, while Ca(2+) stabilizes the disengaged-like form of the loop. |
first_indexed | 2024-04-13T04:45:53Z |
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institution | Directory Open Access Journal |
issn | 1932-6203 |
language | English |
last_indexed | 2024-04-13T04:45:53Z |
publishDate | 2013-01-01 |
publisher | Public Library of Science (PLoS) |
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series | PLoS ONE |
spelling | doaj.art-5761eb16d9744d608d8296b7a3ab48fa2022-12-22T03:01:51ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-01810e7666910.1371/journal.pone.0076669The mechanism of calcium-induced inhibition of muscle fructose 1,6-bisphosphatase and destabilization of glyconeogenic complex.Dariusz RakusAgnieszka GizakAndrzej A KasprzakMarek ZarzyckiEwa Maciaszczyk-DziubinskaAndrzej DzugajThe mechanism by which calcium inhibits the activity of muscle fructose 1,6-bisphosphatase (FBPase) and destabilizes its interaction with aldolase, regulating glycogen synthesis from non-carbohydrates in skeletal muscle is poorly understood. In the current paper, we demonstrate evidence that Ca(2+) affects conformation of the catalytic loop 52-72 of muscle FBPase and inhibits its activity by competing with activatory divalent cations, e.g. Mg(2+) and Zn(2+). We also propose the molecular mechanism of Ca(2+)-induced destabilization of the aldolase-FBPase interaction, showing that aldolase associates with FBPase in its active form, i.e. with loop 52-72 in the engaged conformation, while Ca(2+) stabilizes the disengaged-like form of the loop.http://europepmc.org/articles/PMC3795747?pdf=render |
spellingShingle | Dariusz Rakus Agnieszka Gizak Andrzej A Kasprzak Marek Zarzycki Ewa Maciaszczyk-Dziubinska Andrzej Dzugaj The mechanism of calcium-induced inhibition of muscle fructose 1,6-bisphosphatase and destabilization of glyconeogenic complex. PLoS ONE |
title | The mechanism of calcium-induced inhibition of muscle fructose 1,6-bisphosphatase and destabilization of glyconeogenic complex. |
title_full | The mechanism of calcium-induced inhibition of muscle fructose 1,6-bisphosphatase and destabilization of glyconeogenic complex. |
title_fullStr | The mechanism of calcium-induced inhibition of muscle fructose 1,6-bisphosphatase and destabilization of glyconeogenic complex. |
title_full_unstemmed | The mechanism of calcium-induced inhibition of muscle fructose 1,6-bisphosphatase and destabilization of glyconeogenic complex. |
title_short | The mechanism of calcium-induced inhibition of muscle fructose 1,6-bisphosphatase and destabilization of glyconeogenic complex. |
title_sort | mechanism of calcium induced inhibition of muscle fructose 1 6 bisphosphatase and destabilization of glyconeogenic complex |
url | http://europepmc.org/articles/PMC3795747?pdf=render |
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