Unknown

Dataset Information

0

Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates.


ABSTRACT: Sequence-specific nucleated protein aggregation is closely linked to the pathogenesis of most neurodegenerative diseases and constitutes the molecular basis of prion formation. Here we report that fibrillar polyglutamine peptide aggregates can be internalized by mammalian cells in culture where they gain access to the cytosolic compartment and become co-sequestered in aggresomes together with components of the ubiquitin-proteasome system and cytoplasmic chaperones. Remarkably, these internalized fibrillar aggregates are able to selectively recruit soluble cytoplasmic proteins with which they share homologous but not heterologous amyloidogenic sequences, and to confer a heritable phenotype on cells expressing the homologous amyloidogenic protein from a chromosomal locus.

SUBMITTER: Ren PH 

PROVIDER: S-EPMC2757079 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates.

Ren Pei-Hsien PH   Lauckner Jane E JE   Kachirskaia Ioulia I   Heuser John E JE   Melki Ronald R   Kopito Ron R RR  

Nature cell biology 20090118 2


Sequence-specific nucleated protein aggregation is closely linked to the pathogenesis of most neurodegenerative diseases and constitutes the molecular basis of prion formation. Here we report that fibrillar polyglutamine peptide aggregates can be internalized by mammalian cells in culture where they gain access to the cytosolic compartment and become co-sequestered in aggresomes together with components of the ubiquitin-proteasome system and cytoplasmic chaperones. Remarkably, these internalized  ...[more]

Similar Datasets

| S-EPMC1201602 | biostudies-literature
| S-EPMC18046 | biostudies-literature
| S-EPMC8599886 | biostudies-literature
| S-EPMC2169460 | biostudies-literature
| S-EPMC2265588 | biostudies-literature
| S-EPMC5040113 | biostudies-literature
2022-02-17 | PXD027837 | Pride
| S-EPMC2665101 | biostudies-literature
| S-EPMC151354 | biostudies-literature
| S-EPMC166409 | biostudies-literature