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The ubiquitin ligase Ubr2, a recognition E3 component of the N-end rule pathway, stabilizes Tex19.1 during spermatogenesis

Yang, F and Cheng, Y and An, JY and Kwon, YT and Eckardt, S and Leu, NA and Mclaughlin, KJ and Wang, PJ (2010) The ubiquitin ligase Ubr2, a recognition E3 component of the N-end rule pathway, stabilizes Tex19.1 during spermatogenesis. PLoS ONE, 5 (11).

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Abstract

Ubiquitin E3 ligases target their substrates for ubiquitination, leading to proteasome-mediated degradation or altered biochemical properties. The ubiquitin ligase Ubr2, a recognition E3 component of the N-end rule proteolytic pathway, recognizes proteins with N-terminal destabilizing residues and plays an important role in spermatogenesis. Tex19.1 (also known as Tex19) has been previously identified as a germ cell-specific protein in mouse testis. Here we report that Tex19.1 forms a stable protein complex with Ubr2 in mouse testes. The binding of Tex19.1 to Ubr2 is independent of the second position cysteine of Tex19.1, a putative target for arginylation by the N-end rule pathway R-transferase. The Tex19.1-null mouse mutant phenocopies the Ubr2-deficient mutant in three aspects: heterogeneity of spermatogenic defects, meiotic chromosomal asynapsis, and embryonic lethality preferentially affecting females. In Ubr2-deficient germ cells, Tex19.1 is transcribed, but Tex19.1 protein is absent. Our results suggest that the binding of Ubr2 to Tex19.1 metabolically stabilizes Tex19.1 during spermatogenesis, revealing a new function for Ubr2 outside the conventional N-end rule pathway. © 2010 Yang et al.

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Details

Item Type: Article
Status: Published
Creators/Authors:
CreatorsEmailPitt UsernameORCID
Yang, F
Cheng, Y
An, JY
Kwon, YTyok5@pitt.eduYOK5
Eckardt, S
Leu, NA
Mclaughlin, KJ
Wang, PJ
Contributors:
ContributionContributors NameEmailPitt UsernameORCID
EditorOrban, LaszloUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Date: 3 December 2010
Date Type: Publication
Journal or Publication Title: PLoS ONE
Volume: 5
Number: 11
DOI or Unique Handle: 10.1371/journal.pone.0014017
Refereed: Yes
MeSH Headings: Animals; Binding Sites--genetics; Blotting, Western; Cysteine--genetics; Female; Immunoprecipitation; Male; Methionine--genetics; Mice; Mice, 129 Strain; Mice, Inbred C57BL; Mice, Knockout; NIH 3T3 Cells; Nuclear Proteins--genetics; Nuclear Proteins--metabolism; Protein Binding; Protein Stability; Signal Transduction; Spermatogenesis; Testis--cytology; Testis--metabolism; Ubiquitin-Protein Ligases--genetics; Ubiquitin-Protein Ligases--metabolism
Other ID: NLM PMC2982839
PubMed Central ID: PMC2982839
PubMed ID: 21103378
Date Deposited: 22 Aug 2012 21:54
Last Modified: 04 Feb 2019 15:58
URI: http://d-scholarship.pitt.edu/id/eprint/13576

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