Mutant ubiquitin UBB+1 is accumulated in sporadic inclusion-body myositis muscle fibers

P Fratta; W K Engel; F W Van Leeuwen; E M Hol; G Vattemi; V Askanas

Mutant ubiquitin UBB+1 is accumulated in sporadic inclusion-body myositis muscle fibers

P Fratta
, W K Engel
, F W Van Leeuwen
, E M Hol
, G Vattemi
, V Askanas

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

Mutant ubiquitin (UBB+1), a product of "molecular misreading," is toxic to cells because its ubiquitinated form inhibits the proteasome, contributing to accumulation of misfolded proteins and their ensuing toxicity. The authors demonstrate in 10 sporadic inclusion body myositis (s-IBM) muscle biopsies that UBB+1 is accumulated in aggregates containing amyloid-beta and phosphorylated-tau. In s-IBM, UBB+1 may be pathogenic by inhibiting proteasome, thereby promoting accumulation of cytotoxic misfolded amyloid-beta and phosphorylated-tau.

Original language	English
Pages (from-to)	1114-7
Number of pages	4
Journal	Neurology
Volume	63
Issue number	6
Publication status	Published - 28 Sept 2004

Keywords

Amino Acid Sequence
Amyloid beta-Peptides
Biopsy
Humans
Microscopy, Fluorescence
Microscopy, Immunoelectron
Molecular Sequence Data
Muscle Fibers, Skeletal
Muscular Diseases
Myositis, Inclusion Body
Phosphorylation
Proteasome Inhibitors
Protein Folding
Protein Processing, Post-Translational
Ubiquitin
tau Proteins
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.

Cite this

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title = "Mutant ubiquitin UBB+1 is accumulated in sporadic inclusion-body myositis muscle fibers",

abstract = "Mutant ubiquitin (UBB+1), a product of {"}molecular misreading,{"} is toxic to cells because its ubiquitinated form inhibits the proteasome, contributing to accumulation of misfolded proteins and their ensuing toxicity. The authors demonstrate in 10 sporadic inclusion body myositis (s-IBM) muscle biopsies that UBB+1 is accumulated in aggregates containing amyloid-beta and phosphorylated-tau. In s-IBM, UBB+1 may be pathogenic by inhibiting proteasome, thereby promoting accumulation of cytotoxic misfolded amyloid-beta and phosphorylated-tau.",

keywords = "Amino Acid Sequence, Amyloid beta-Peptides, Biopsy, Humans, Microscopy, Fluorescence, Microscopy, Immunoelectron, Molecular Sequence Data, Muscle Fibers, Skeletal, Muscular Diseases, Myositis, Inclusion Body, Phosphorylation, Proteasome Inhibitors, Protein Folding, Protein Processing, Post-Translational, Ubiquitin, tau Proteins, Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S., Research Support, U.S. Gov't, P.H.S.",

author = "P Fratta and Engel, \{W K\} and \{Van Leeuwen\}, \{F W\} and Hol, \{E M\} and G Vattemi and V Askanas",

year = "2004",

month = sep,

day = "28",

language = "English",

volume = "63",

pages = "1114--7",

journal = "Neurology",

issn = "0028-3878",

publisher = "Lippincott Williams \& Wilkins",

number = "6",

}

TY - JOUR

T1 - Mutant ubiquitin UBB+1 is accumulated in sporadic inclusion-body myositis muscle fibers

AU - Fratta, P

AU - Engel, W K

AU - Van Leeuwen, F W

AU - Hol, E M

AU - Vattemi, G

AU - Askanas, V

PY - 2004/9/28

Y1 - 2004/9/28

N2 - Mutant ubiquitin (UBB+1), a product of "molecular misreading," is toxic to cells because its ubiquitinated form inhibits the proteasome, contributing to accumulation of misfolded proteins and their ensuing toxicity. The authors demonstrate in 10 sporadic inclusion body myositis (s-IBM) muscle biopsies that UBB+1 is accumulated in aggregates containing amyloid-beta and phosphorylated-tau. In s-IBM, UBB+1 may be pathogenic by inhibiting proteasome, thereby promoting accumulation of cytotoxic misfolded amyloid-beta and phosphorylated-tau.

AB - Mutant ubiquitin (UBB+1), a product of "molecular misreading," is toxic to cells because its ubiquitinated form inhibits the proteasome, contributing to accumulation of misfolded proteins and their ensuing toxicity. The authors demonstrate in 10 sporadic inclusion body myositis (s-IBM) muscle biopsies that UBB+1 is accumulated in aggregates containing amyloid-beta and phosphorylated-tau. In s-IBM, UBB+1 may be pathogenic by inhibiting proteasome, thereby promoting accumulation of cytotoxic misfolded amyloid-beta and phosphorylated-tau.

KW - Amino Acid Sequence

KW - Amyloid beta-Peptides

KW - Biopsy

KW - Humans

KW - Microscopy, Fluorescence

KW - Microscopy, Immunoelectron

KW - Molecular Sequence Data

KW - Muscle Fibers, Skeletal

KW - Muscular Diseases

KW - Myositis, Inclusion Body

KW - Phosphorylation

KW - Proteasome Inhibitors

KW - Protein Folding

KW - Protein Processing, Post-Translational

KW - Ubiquitin

KW - tau Proteins

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

KW - Research Support, U.S. Gov't, Non-P.H.S.

KW - Research Support, U.S. Gov't, P.H.S.

M3 - Article

C2 - 15452314

SN - 0028-3878

VL - 63

SP - 1114

EP - 1117

JO - Neurology

JF - Neurology

IS - 6

ER -

Mutant ubiquitin UBB+1 is accumulated in sporadic inclusion-body myositis muscle fibers

Abstract

Keywords

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