Bmcc1s, a novel brain-isoform of Bmcc1, affects cell morphology by regulating MAP6/STOP functions.
The BCH (BNIP2 and Cdc42GAP Homology) domain-containing protein Bmcc1/Prune2 is highly enriched in the brain and is involved in the regulation of cytoskeleton dynamics and cell survival. However, the molecular mechanisms accounting for these functions are poorly defined. Here, we have identified Bmc...
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2012-01-01
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doaj-e51c91d553ac40cab30b6868adc047fc2020-11-25T01:45:55ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-0174e3548810.1371/journal.pone.0035488Bmcc1s, a novel brain-isoform of Bmcc1, affects cell morphology by regulating MAP6/STOP functions.Jessica AramaAnne-Cécile BoulayChristophe BoscChristian DelphinDamarys LoewPhilippe RostaingEdwige AmigouPascal EzanLaure WingertsmannLaurent GuillaudAnnie AndrieuxChristian GiaumeMartine Cohen-SalmonThe BCH (BNIP2 and Cdc42GAP Homology) domain-containing protein Bmcc1/Prune2 is highly enriched in the brain and is involved in the regulation of cytoskeleton dynamics and cell survival. However, the molecular mechanisms accounting for these functions are poorly defined. Here, we have identified Bmcc1s, a novel isoform of Bmcc1 predominantly expressed in the mouse brain. In primary cultures of astrocytes and neurons, Bmcc1s localized on intermediate filaments and microtubules and interacted directly with MAP6/STOP, a microtubule-binding protein responsible for microtubule cold stability. Bmcc1s overexpression inhibited MAP6-induced microtubule cold stability by displacing MAP6 away from microtubules. It also resulted in the formation of membrane protrusions for which MAP6 was a necessary cofactor of Bmcc1s. This study identifies Bmcc1s as a new MAP6 interacting protein able to modulate MAP6-induced microtubule cold stability. Moreover, it illustrates a novel mechanism by which Bmcc1 regulates cell morphology.http://europepmc.org/articles/PMC3327665?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Jessica Arama Anne-Cécile Boulay Christophe Bosc Christian Delphin Damarys Loew Philippe Rostaing Edwige Amigou Pascal Ezan Laure Wingertsmann Laurent Guillaud Annie Andrieux Christian Giaume Martine Cohen-Salmon |
spellingShingle |
Jessica Arama Anne-Cécile Boulay Christophe Bosc Christian Delphin Damarys Loew Philippe Rostaing Edwige Amigou Pascal Ezan Laure Wingertsmann Laurent Guillaud Annie Andrieux Christian Giaume Martine Cohen-Salmon Bmcc1s, a novel brain-isoform of Bmcc1, affects cell morphology by regulating MAP6/STOP functions. PLoS ONE |
author_facet |
Jessica Arama Anne-Cécile Boulay Christophe Bosc Christian Delphin Damarys Loew Philippe Rostaing Edwige Amigou Pascal Ezan Laure Wingertsmann Laurent Guillaud Annie Andrieux Christian Giaume Martine Cohen-Salmon |
author_sort |
Jessica Arama |
title |
Bmcc1s, a novel brain-isoform of Bmcc1, affects cell morphology by regulating MAP6/STOP functions. |
title_short |
Bmcc1s, a novel brain-isoform of Bmcc1, affects cell morphology by regulating MAP6/STOP functions. |
title_full |
Bmcc1s, a novel brain-isoform of Bmcc1, affects cell morphology by regulating MAP6/STOP functions. |
title_fullStr |
Bmcc1s, a novel brain-isoform of Bmcc1, affects cell morphology by regulating MAP6/STOP functions. |
title_full_unstemmed |
Bmcc1s, a novel brain-isoform of Bmcc1, affects cell morphology by regulating MAP6/STOP functions. |
title_sort |
bmcc1s, a novel brain-isoform of bmcc1, affects cell morphology by regulating map6/stop functions. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2012-01-01 |
description |
The BCH (BNIP2 and Cdc42GAP Homology) domain-containing protein Bmcc1/Prune2 is highly enriched in the brain and is involved in the regulation of cytoskeleton dynamics and cell survival. However, the molecular mechanisms accounting for these functions are poorly defined. Here, we have identified Bmcc1s, a novel isoform of Bmcc1 predominantly expressed in the mouse brain. In primary cultures of astrocytes and neurons, Bmcc1s localized on intermediate filaments and microtubules and interacted directly with MAP6/STOP, a microtubule-binding protein responsible for microtubule cold stability. Bmcc1s overexpression inhibited MAP6-induced microtubule cold stability by displacing MAP6 away from microtubules. It also resulted in the formation of membrane protrusions for which MAP6 was a necessary cofactor of Bmcc1s. This study identifies Bmcc1s as a new MAP6 interacting protein able to modulate MAP6-induced microtubule cold stability. Moreover, it illustrates a novel mechanism by which Bmcc1 regulates cell morphology. |
url |
http://europepmc.org/articles/PMC3327665?pdf=render |
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