Toxic PR Poly-Dipeptides Encoded by the C9orf72 Repeat Expansion Target LC Domain Polymers | Zendy

Yi Lin | Zendy; Eiichiro Mori | Zendy; Masato Kato | Zendy; Siheng Xiang | Zendy; Leeju C. Wu | Zendy; Ilmin Kwon | Zendy; Steven L. McKnight | Zendy

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Toxic PR Poly-Dipeptides Encoded by the C9orf72 Repeat Expansion Target LC Domain Polymers

Author(s) -

Yi Lin,

Eiichiro Mori,

Masato Kato,

Siheng Xiang,

Leeju C. Wu,

Ilmin Kwon,

Steven L. McKnight

Publication year - 2016

Publication title -

cell

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 26.304

H-Index - 776

eISSN - 1097-4172

pISSN - 0092-8674

DOI - 10.1016/j.cell.2016.10.003

Subject(s) - biology , c9orf72 , dipeptide , organelle , microbiology and biotechnology , gene , amyotrophic lateral sclerosis , computational biology , biophysics , biochemistry , genetics , trinucleotide repeat expansion , amino acid , medicine , allele , disease , pathology

Two complementary approaches were used in search of the intracellular targets of the toxic PR poly-dipeptide encoded by the repeat sequences expanded in the C9orf72 form of amyotrophic lateral sclerosis. The top categories of PR n -bound proteins include constituents of non-membrane invested cellular organelles and intermediate filaments. PR n targets are enriched for the inclusion of low complexity (LC) sequences. Evidence is presented indicating that LC sequences represent the direct target of PR n binding and that interaction between the PR n poly-dipeptide and LC domains is polymer-dependent. These studies indicate that PR n -mediated toxicity may result from broad impediments to the dynamics of cell structure and information flow from gene to message to protein.

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