Ubiquilin 2 is not associated with tau pathology.

Accumulation of aberrant proteins in inclusion bodies is a hallmark of many neurodegenerative diseases. Impairment of proteolytic systems is a common event in these protein misfolding diseases. Recently, mutations in the UBQLN 2 gene encoding ubiquilin 2 have been identified in X-linked amyotrophic...

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Autores principales:	Anna Nölle, Elise S van Haastert, Rob Zwart, Jeroen J M Hoozemans, Wiep Scheper
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/2719d79120574f6b8ca927c7c96396a4
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spelling	oai:doaj.org-article:2719d79120574f6b8ca927c7c96396a42021-11-18T08:53:40ZUbiquilin 2 is not associated with tau pathology.1932-620310.1371/journal.pone.0076598https://doaj.org/article/2719d79120574f6b8ca927c7c96396a42013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24086754/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Accumulation of aberrant proteins in inclusion bodies is a hallmark of many neurodegenerative diseases. Impairment of proteolytic systems is a common event in these protein misfolding diseases. Recently, mutations in the UBQLN 2 gene encoding ubiquilin 2 have been identified in X-linked amyotrophic lateral sclerosis (ALS). Furthermore, ubiquilin 2 is associated with inclusions in familial and sporadic ALS/dementia, synucleinopathies and polyglutamine diseases. Ubiquilin 2 exerts a regulatory role in proteostasis and thus it has been suggested that ubiquilin 2 pathology may be a common event in neurodegenerative diseases. Tauopathies, a heterogenous group of neurodegenerative diseases accompanied with dementia, are characterized by inclusions of the microtubule-binding protein tau. In the present study, we investigate whether ubiquilin 2 is connected with tau pathology in Alzheimer's disease (AD), supranuclear palsy (PSP) and Pick's disease (PiD) and familial cases with frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17). We show that ubiquilin 2 positive inclusions are absent in these tauopathies. Furthermore, we find decreased ubiquilin 2 protein levels in AD patients, but our results do not indicate a correlation with tau pathology. Our data show no evidence for involvement of ubiquilin 2 and indicate that other mechanisms underly the proteostatic disturbances in tauopathies.Anna NölleElise S van HaastertRob ZwartJeroen J M HoozemansWiep ScheperPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 9, p e76598 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Anna Nölle Elise S van Haastert Rob Zwart Jeroen J M Hoozemans Wiep Scheper Ubiquilin 2 is not associated with tau pathology.
description	Accumulation of aberrant proteins in inclusion bodies is a hallmark of many neurodegenerative diseases. Impairment of proteolytic systems is a common event in these protein misfolding diseases. Recently, mutations in the UBQLN 2 gene encoding ubiquilin 2 have been identified in X-linked amyotrophic lateral sclerosis (ALS). Furthermore, ubiquilin 2 is associated with inclusions in familial and sporadic ALS/dementia, synucleinopathies and polyglutamine diseases. Ubiquilin 2 exerts a regulatory role in proteostasis and thus it has been suggested that ubiquilin 2 pathology may be a common event in neurodegenerative diseases. Tauopathies, a heterogenous group of neurodegenerative diseases accompanied with dementia, are characterized by inclusions of the microtubule-binding protein tau. In the present study, we investigate whether ubiquilin 2 is connected with tau pathology in Alzheimer's disease (AD), supranuclear palsy (PSP) and Pick's disease (PiD) and familial cases with frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17). We show that ubiquilin 2 positive inclusions are absent in these tauopathies. Furthermore, we find decreased ubiquilin 2 protein levels in AD patients, but our results do not indicate a correlation with tau pathology. Our data show no evidence for involvement of ubiquilin 2 and indicate that other mechanisms underly the proteostatic disturbances in tauopathies.
format	article
author	Anna Nölle Elise S van Haastert Rob Zwart Jeroen J M Hoozemans Wiep Scheper
author_facet	Anna Nölle Elise S van Haastert Rob Zwart Jeroen J M Hoozemans Wiep Scheper
author_sort	Anna Nölle
title	Ubiquilin 2 is not associated with tau pathology.
title_short	Ubiquilin 2 is not associated with tau pathology.
title_full	Ubiquilin 2 is not associated with tau pathology.
title_fullStr	Ubiquilin 2 is not associated with tau pathology.
title_full_unstemmed	Ubiquilin 2 is not associated with tau pathology.
title_sort	ubiquilin 2 is not associated with tau pathology.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/2719d79120574f6b8ca927c7c96396a4
work_keys_str_mv	AT annanolle ubiquilin2isnotassociatedwithtaupathology AT elisesvanhaastert ubiquilin2isnotassociatedwithtaupathology AT robzwart ubiquilin2isnotassociatedwithtaupathology AT jeroenjmhoozemans ubiquilin2isnotassociatedwithtaupathology AT wiepscheper ubiquilin2isnotassociatedwithtaupathology
_version_	1718421190737920000

Ubiquilin 2 is not associated with tau pathology.

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