Cargando…

Dynamic scaffolds for neuronal signaling: in silico analysis of the TANC protein family

The emergence of genes implicated across multiple comorbid neurologic disorders allows to identify shared underlying molecular pathways. Recently, investigation of patients with diverse neurologic disorders found TANC1 and TANC2 as possible candidate disease genes. While the TANC proteins have been...

Descripción completa

Detalles Bibliográficos
Autores principales: Gasparini, Alessandra, Tosatto, Silvio C. E., Murgia, Alessandra, Leonardi, Emanuela
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5533708/
https://www.ncbi.nlm.nih.gov/pubmed/28754924
http://dx.doi.org/10.1038/s41598-017-05748-5
_version_ 1783253650937741312
author Gasparini, Alessandra
Tosatto, Silvio C. E.
Murgia, Alessandra
Leonardi, Emanuela
author_facet Gasparini, Alessandra
Tosatto, Silvio C. E.
Murgia, Alessandra
Leonardi, Emanuela
author_sort Gasparini, Alessandra
collection PubMed
description The emergence of genes implicated across multiple comorbid neurologic disorders allows to identify shared underlying molecular pathways. Recently, investigation of patients with diverse neurologic disorders found TANC1 and TANC2 as possible candidate disease genes. While the TANC proteins have been reported as postsynaptic scaffolds influencing synaptic spines and excitatory synapse strength, their molecular functions remain unknown. Here, we conducted a comprehensive in silico analysis of the TANC protein family to characterize their molecular role and understand possible neurobiological consequences of their disruption. The known Ankyrin and tetratricopeptide repeat (TPR) domains have been modeled. The newly predicted N-terminal ATPase domain may function as a regulated molecular switch for downstream signaling. Several putative conserved protein binding motifs allowed to extend the TANC interaction network. Interestingly, we highlighted connections with different signaling pathways converging to modulate neuronal activity. Beyond a known role for TANC family members in the glutamate receptor pathway, they seem linked to planar cell polarity signaling, Hippo pathway, and cilium assembly. This suggests an important role in neuron projection, extension and differentiation.
format Online
Article
Text
id pubmed-5533708
institution National Center for Biotechnology Information
language English
publishDate 2017
publisher Nature Publishing Group UK
record_format MEDLINE/PubMed
spelling pubmed-55337082017-08-03 Dynamic scaffolds for neuronal signaling: in silico analysis of the TANC protein family Gasparini, Alessandra Tosatto, Silvio C. E. Murgia, Alessandra Leonardi, Emanuela Sci Rep Article The emergence of genes implicated across multiple comorbid neurologic disorders allows to identify shared underlying molecular pathways. Recently, investigation of patients with diverse neurologic disorders found TANC1 and TANC2 as possible candidate disease genes. While the TANC proteins have been reported as postsynaptic scaffolds influencing synaptic spines and excitatory synapse strength, their molecular functions remain unknown. Here, we conducted a comprehensive in silico analysis of the TANC protein family to characterize their molecular role and understand possible neurobiological consequences of their disruption. The known Ankyrin and tetratricopeptide repeat (TPR) domains have been modeled. The newly predicted N-terminal ATPase domain may function as a regulated molecular switch for downstream signaling. Several putative conserved protein binding motifs allowed to extend the TANC interaction network. Interestingly, we highlighted connections with different signaling pathways converging to modulate neuronal activity. Beyond a known role for TANC family members in the glutamate receptor pathway, they seem linked to planar cell polarity signaling, Hippo pathway, and cilium assembly. This suggests an important role in neuron projection, extension and differentiation. Nature Publishing Group UK 2017-07-28 /pmc/articles/PMC5533708/ /pubmed/28754924 http://dx.doi.org/10.1038/s41598-017-05748-5 Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Gasparini, Alessandra
Tosatto, Silvio C. E.
Murgia, Alessandra
Leonardi, Emanuela
Dynamic scaffolds for neuronal signaling: in silico analysis of the TANC protein family
title Dynamic scaffolds for neuronal signaling: in silico analysis of the TANC protein family
title_full Dynamic scaffolds for neuronal signaling: in silico analysis of the TANC protein family
title_fullStr Dynamic scaffolds for neuronal signaling: in silico analysis of the TANC protein family
title_full_unstemmed Dynamic scaffolds for neuronal signaling: in silico analysis of the TANC protein family
title_short Dynamic scaffolds for neuronal signaling: in silico analysis of the TANC protein family
title_sort dynamic scaffolds for neuronal signaling: in silico analysis of the tanc protein family
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5533708/
https://www.ncbi.nlm.nih.gov/pubmed/28754924
http://dx.doi.org/10.1038/s41598-017-05748-5
work_keys_str_mv AT gasparinialessandra dynamicscaffoldsforneuronalsignalinginsilicoanalysisofthetancproteinfamily
AT tosattosilvioce dynamicscaffoldsforneuronalsignalinginsilicoanalysisofthetancproteinfamily
AT murgiaalessandra dynamicscaffoldsforneuronalsignalinginsilicoanalysisofthetancproteinfamily
AT leonardiemanuela dynamicscaffoldsforneuronalsignalinginsilicoanalysisofthetancproteinfamily