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DAPLE and MPDZ bind to each other and cooperate to promote apical cell constriction

Dishevelled-Associating Protein with a high frequency of LEucines (DAPLE) belongs to a group of unconventional activators of heterotrimeric G-proteins that are cytoplasmic factors rather than membrane proteins of the G-protein–coupled receptor superfamily. During neurulation, DAPLE localizes to apic...

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Autores principales: Marivin, Arthur, Garcia-Marcos, Mikel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6727773/
https://www.ncbi.nlm.nih.gov/pubmed/31268831
http://dx.doi.org/10.1091/mbc.E19-02-0091
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author Marivin, Arthur
Garcia-Marcos, Mikel
author_facet Marivin, Arthur
Garcia-Marcos, Mikel
author_sort Marivin, Arthur
collection PubMed
description Dishevelled-Associating Protein with a high frequency of LEucines (DAPLE) belongs to a group of unconventional activators of heterotrimeric G-proteins that are cytoplasmic factors rather than membrane proteins of the G-protein–coupled receptor superfamily. During neurulation, DAPLE localizes to apical junctions of neuroepithelial cells and promotes apical cell constriction via G-protein activation. While junctional localization of DAPLE is necessary for this function, the factors it associates with at apical junctions or how they contribute to DAPLE-mediated apical constriction are unknown. MPDZ is a multi-PDZ (PSD95/DLG1/ZO-1) domain scaffold present at apical cell junctions whose mutation in humans is linked to nonsyndromic congenital hydrocephalus (NSCH). DAPLE contains a PDZ-binding motif (PBM) and is also mutated in human NSCH, so we investigated the functional relationship between both proteins. DAPLE colocalized with MPDZ at apical cell junctions and bound directly to the PDZ3 domain of MPDZ via its PBM. Much like DAPLE, MPDZ is induced during neurulation in Xenopus and is required for apical constriction of neuroepithelial cells and subsequent neural plate bending. MPDZ depletion also blunted DAPLE-­mediated apical constriction of cultured cells. These results show that DAPLE and MPDZ, two factors genetically linked to NSCH, function as cooperative partners at apical junctions and are required for proper tissue remodeling during early stages of neurodevelopment.
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spelling pubmed-67277732019-10-07 DAPLE and MPDZ bind to each other and cooperate to promote apical cell constriction Marivin, Arthur Garcia-Marcos, Mikel Mol Biol Cell Brief Reports Dishevelled-Associating Protein with a high frequency of LEucines (DAPLE) belongs to a group of unconventional activators of heterotrimeric G-proteins that are cytoplasmic factors rather than membrane proteins of the G-protein–coupled receptor superfamily. During neurulation, DAPLE localizes to apical junctions of neuroepithelial cells and promotes apical cell constriction via G-protein activation. While junctional localization of DAPLE is necessary for this function, the factors it associates with at apical junctions or how they contribute to DAPLE-mediated apical constriction are unknown. MPDZ is a multi-PDZ (PSD95/DLG1/ZO-1) domain scaffold present at apical cell junctions whose mutation in humans is linked to nonsyndromic congenital hydrocephalus (NSCH). DAPLE contains a PDZ-binding motif (PBM) and is also mutated in human NSCH, so we investigated the functional relationship between both proteins. DAPLE colocalized with MPDZ at apical cell junctions and bound directly to the PDZ3 domain of MPDZ via its PBM. Much like DAPLE, MPDZ is induced during neurulation in Xenopus and is required for apical constriction of neuroepithelial cells and subsequent neural plate bending. MPDZ depletion also blunted DAPLE-­mediated apical constriction of cultured cells. These results show that DAPLE and MPDZ, two factors genetically linked to NSCH, function as cooperative partners at apical junctions and are required for proper tissue remodeling during early stages of neurodevelopment. The American Society for Cell Biology 2019-07-22 /pmc/articles/PMC6727773/ /pubmed/31268831 http://dx.doi.org/10.1091/mbc.E19-02-0091 Text en © 2019 Marivin and Garcia-Marcos. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. http://creativecommons.org/licenses/by-nc-sa/3.0 This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License.
spellingShingle Brief Reports
Marivin, Arthur
Garcia-Marcos, Mikel
DAPLE and MPDZ bind to each other and cooperate to promote apical cell constriction
title DAPLE and MPDZ bind to each other and cooperate to promote apical cell constriction
title_full DAPLE and MPDZ bind to each other and cooperate to promote apical cell constriction
title_fullStr DAPLE and MPDZ bind to each other and cooperate to promote apical cell constriction
title_full_unstemmed DAPLE and MPDZ bind to each other and cooperate to promote apical cell constriction
title_short DAPLE and MPDZ bind to each other and cooperate to promote apical cell constriction
title_sort daple and mpdz bind to each other and cooperate to promote apical cell constriction
topic Brief Reports
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6727773/
https://www.ncbi.nlm.nih.gov/pubmed/31268831
http://dx.doi.org/10.1091/mbc.E19-02-0091
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