Emerging roles of TRIO and F-actin-binding protein in human diseases

TRIO and F-actin-binding protein (TRIOBP) also referred to as Tara, was originally isolated as a cytoskeleton remodeling protein. TRIOBP-1 is important for regulating F-actin filament reorganization. TRIOBP variants are broadly classified as variant-1 or − 4 and do not share exons. TRIOBP variant-5...

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Autores principales: Park, Sungjin, Lee, Hyunji, Kim, Minhee, Park, Jisoo, Kim, Seon-Hwan, Park, Jongsun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2018
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5996455/
https://www.ncbi.nlm.nih.gov/pubmed/29890989
http://dx.doi.org/10.1186/s12964-018-0237-y
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author Park, Sungjin
Lee, Hyunji
Kim, Minhee
Park, Jisoo
Kim, Seon-Hwan
Park, Jongsun
author_facet Park, Sungjin
Lee, Hyunji
Kim, Minhee
Park, Jisoo
Kim, Seon-Hwan
Park, Jongsun
author_sort Park, Sungjin
collection PubMed
description TRIO and F-actin-binding protein (TRIOBP) also referred to as Tara, was originally isolated as a cytoskeleton remodeling protein. TRIOBP-1 is important for regulating F-actin filament reorganization. TRIOBP variants are broadly classified as variant-1 or − 4 and do not share exons. TRIOBP variant-5 contains all exons. Earlier studies indicated that TRIOBP-4/5 mutation is a pivotal element of autosomal recessive nonsyndromic hearing loss. However, recent studies provide clues that TRIOBP variants are associated with other human diseases including cancer and brain diseases. In this review, recent functional studies focusing on TRIOBP variants and its possible disease models are described.
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spelling pubmed-59964552018-06-25 Emerging roles of TRIO and F-actin-binding protein in human diseases Park, Sungjin Lee, Hyunji Kim, Minhee Park, Jisoo Kim, Seon-Hwan Park, Jongsun Cell Commun Signal Review TRIO and F-actin-binding protein (TRIOBP) also referred to as Tara, was originally isolated as a cytoskeleton remodeling protein. TRIOBP-1 is important for regulating F-actin filament reorganization. TRIOBP variants are broadly classified as variant-1 or − 4 and do not share exons. TRIOBP variant-5 contains all exons. Earlier studies indicated that TRIOBP-4/5 mutation is a pivotal element of autosomal recessive nonsyndromic hearing loss. However, recent studies provide clues that TRIOBP variants are associated with other human diseases including cancer and brain diseases. In this review, recent functional studies focusing on TRIOBP variants and its possible disease models are described. BioMed Central 2018-06-11 /pmc/articles/PMC5996455/ /pubmed/29890989 http://dx.doi.org/10.1186/s12964-018-0237-y Text en © The Author(s). 2018 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Review
Park, Sungjin
Lee, Hyunji
Kim, Minhee
Park, Jisoo
Kim, Seon-Hwan
Park, Jongsun
Emerging roles of TRIO and F-actin-binding protein in human diseases
title Emerging roles of TRIO and F-actin-binding protein in human diseases
title_full Emerging roles of TRIO and F-actin-binding protein in human diseases
title_fullStr Emerging roles of TRIO and F-actin-binding protein in human diseases
title_full_unstemmed Emerging roles of TRIO and F-actin-binding protein in human diseases
title_short Emerging roles of TRIO and F-actin-binding protein in human diseases
title_sort emerging roles of trio and f-actin-binding protein in human diseases
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5996455/
https://www.ncbi.nlm.nih.gov/pubmed/29890989
http://dx.doi.org/10.1186/s12964-018-0237-y
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