Identities of Sequestered Proteins in Aggregates from Cells with Induced Polyglutamine Expression

Proteins with expanded polyglutamine (polyQ) tracts have been linked to neurodegenerative diseases. One common characteristic of expanded-polyQ expression is the formation of intracellular aggregates (IAs). IAs purified from polyQ-expressing cells were dissociated and studied by protein blot assay a...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of cell biology 2001-04, Vol.153 (2), p.283-294
Main Authors: Suhr, Steven T., Senut, Marie-Claude, Whitelegge, Julian P., Faull, Kym F., Cuizon, Denise B., Gage, Fred H.
Format: Article
Language:English
Subjects:
Actins
Actins - metabolism
Aged
Antibodies
Cell aggregates
Cell extracts
Cell Line
Cell lines
Cell Size
Cells
Cellular biology
Corpus Striatum - cytology
Disease
DNA-Binding Proteins - metabolism
Gels
Genes, Reporter
HEK293 cells
HSP70 Heat-Shock Proteins - metabolism
Humans
Huntingtin Protein
In Situ Nick-End Labeling
Microscopy, Fluorescence
Middle Aged
Molecular weight
Nerve Tissue Proteins - genetics
Nerve Tissue Proteins - metabolism
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Original
Peptides - genetics
Peptides - metabolism
Proteins
Recombinant Fusion Proteins - metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
TATA-Box Binding Protein
Transcription Factors - metabolism
Transfection
Ubiquitins
Ubiquitins - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Proteins with expanded polyglutamine (polyQ) tracts have been linked to neurodegenerative diseases. One common characteristic of expanded-polyQ expression is the formation of intracellular aggregates (IAs). IAs purified from polyQ-expressing cells were dissociated and studied by protein blot assay and mass spectrometry to determine the identity, condition, and relative level of several proteins sequestered within aggregates. Most of the sequestered proteins comigrated with bands from control extracts, indicating that the sequestered proteins were intact and not irreversibly bound to the polyQ polymer. Among the proteins found sequestered at relatively high levels in purified IAs were ubiquitin, the cell cycle-regulating proteins p53 and mdm-2, HSP70, the global transcriptional regulator Tata-binding protein/TFIID, cytoskeleton proteins actin and 68-kD neurofilament, and proteins of the nuclear pore complex. These data reveal that IAs are highly complex structures with a multiplicity of contributing proteins.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.153.2.283