Differential recruitment of UBQLN2 to nuclear inclusions in the polyglutamine diseases HD and SCA3

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Differential recruitment of UBQLN2 to nuclear inclusions in the polyglutamine diseases HD and SCA3

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作者：Li Zeng^a ; Bo Wang^a ; Sean A. Merillat^a ; Eiko N. Minakawa^b ; Matthew D. Perkins^c ; Biswarathan Ramani^a ; Sara J. Tallaksen-Greene^a ; Maria do Carmo Costa^a ; Roger L. Albin^a ; ^d ; Henry L. Paulson^a ; ^{henryp@umich.edu" class="auth_mail" title="E-mail the corresponding author}
关键词：polyQ ; polyglutamine ; HD ; Huntington's disease ; HTT ; Huntingtin protein ; SCA3 ; spinocerebellar ataxia type 3 ; UPP ; ubiquitin&ndash ; proteasome pathway ; UBL ; ubiquitin-like domain ; UBA ; ubiquitin-associated domain ; PLIC-1 ; integrin-associated protein and cytoskeleton-1 ; SCA3-KI ; SCA3 knock-in mouse ; HD-KI (Q200) ; Huntingtin knock-in mouse with 200 CAG repeats ; HD-KI (Q150) ; Huntingtin knock-in mouse with 150 CAG repeats ; SCA3 YAC ; SCA3 YACMJD84 transgenic mouse ; AD ; Alzheimer's disease ; APP ; Amylo
刊名：Neurobiology of Disease
出版年：2015
出版时间：October 2015
年：2015
卷：82
期：Complete
页码：281-288
全文大小：2130 K

文摘

class="label">•: UBQLN2 localizes to aggregates in mouse models of HD but not SCA3.
class="label">•: Early recruitment of UBQLN2 to inclusions in HD-KI mice
class="label">•: UBQLN2-positive aggregates in human HD brain but not in SCA3 brain
class="label">•: HTT, the HD disease protein, rather than ATXN3, the SCA3 disease protein interacts with UBQLN2.

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