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The E3 ligase Listerin/Ltn1 links ribosome‐associated protein quality control and neurodegeneration
Author(s) -
Joazeiro Claudio
Publication year - 2016
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.30.1_supplement.391.3
Subject(s) - ubiquitin ligase , ribosome , neurodegeneration , biology , microbiology and biotechnology , translation (biology) , protein subunit , dna ligase , ubiquitin , ribosomal protein , genetics , computational biology , gene , rna , messenger rna , medicine , disease , pathology
We had previously reported that a homozygous mutation in the lister gene leads to neurodegeneration in mice. lister encodes a RING domain E3 ligase, Listerin, which is conserved among eukaryotic organisms and is widely expressed in mouse tissues. To elucidate Listerin's function we took advantage of the genetic and biochemical tractability of S. cerevisiae and discovered that the yeast Listerin ortholog (Ltn1) is a key player in a novel pathway of protein quality control; more specifically, Ltn1 associates with the 60S ribosomal subunit, and acts as the critical E3 ligase mediating degradation of aberrant nascent polypeptides remaining stalled on ribosomes that are unable to either elongate or terminate translation (2, 3). Subsequent work from others revealed that Ltn1 functions together with other factors as part of the Ribosome‐Associated Quality Control (RQC) complex. I will present ongoing work in the lab towards dissecting mechanisms underlying Ltn1 and RQC function. Support or Funding Information