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Literature DB >> 26123109

How cells coordinate waste removal through their major proteolytic pathways.

Abstract

The eukaryotic cell uses two complex machineries to degrade unwanted proteins. The first is the ubiquitin-proteasome system and the second is autophagy. A new study contributes to our understanding of how the two systems interconnect to coordinate protein degradation.

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Year: 2015 PMID： 26123109 DOI： 10.1038/ncb3198

Source DB: PubMed Journal: Nat Cell Biol ISSN： 1465-7392 Impact factor: 28.824

12 in total

Review 1. Selective autophagy mediated by autophagic adapter proteins.

Authors: Terje Johansen; Trond Lamark
Journal: Autophagy Date: 2011-03 Impact factor: 16.016

Review 2. Regulated protein turnover: snapshots of the proteasome in action.

Authors: Sucharita Bhattacharyya; Houqing Yu; Carsten Mim; Andreas Matouschek
Journal: Nat Rev Mol Cell Biol Date: 2014-02 Impact factor: 94.444

Review 3. The N-end rule pathway and regulation by proteolysis.

Authors: Alexander Varshavsky
Journal: Protein Sci Date: 2011-08 Impact factor: 6.725

4. In vivo half-life of a protein is a function of its amino-terminal residue.

Authors: A Bachmair; D Finley; A Varshavsky
Journal: Science Date: 1986-10-10 Impact factor: 47.728

5. Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy.

Authors: K B Kegel; M Kim; E Sapp; C McIntyre; J G Castaño; N Aronin; M DiFiglia
Journal: J Neurosci Date: 2000-10-01 Impact factor: 6.167

Review 6. The eukaryotic N-end rule pathway: conserved mechanisms and diverse functions.

Authors: Daniel J Gibbs; Jaume Bacardit; Andreas Bachmair; Michael J Holdsworth
Journal: Trends Cell Biol Date: 2014-05-26 Impact factor: 20.808

7. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death.

Authors: Geir Bjørkøy; Trond Lamark; Andreas Brech; Heidi Outzen; Maria Perander; Aud Overvatn; Harald Stenmark; Terje Johansen
Journal: J Cell Biol Date: 2005-11-14 Impact factor: 10.539

8. Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding.

Authors: Hyunjoo Cha-Molstad; Ki Sa Sung; Joonsung Hwang; Kyoung A Kim; Ji Eun Yu; Young Dong Yoo; Jun Min Jang; Dong Hoon Han; Michael Molstad; Jung Gi Kim; Yoon Jee Lee; Adriana Zakrzewska; Su-Hyeon Kim; Sung Tae Kim; Sun Yong Kim; Hee Gu Lee; Nak Kyun Soung; Jong Seog Ahn; Aaron Ciechanover; Bo Yeon Kim; Yong Tae Kwon
Journal: Nat Cell Biol Date: 2015-06-15 Impact factor: 28.824

How cells coordinate waste removal through their major proteolytic pathways.

Review 1. Selective autophagy mediated by autophagic adapter proteins.

Review 2. Regulated protein turnover: snapshots of the proteasome in action.

Review 3. The N-end rule pathway and regulation by proteolysis.

4. In vivo half-life of a protein is a function of its amino-terminal residue.

5. Huntingtin expression stimulates endosomal-lysosomal activity, endosome tubulation, and autophagy.

Review 6. The eukaryotic N-end rule pathway: conserved mechanisms and diverse functions.

7. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death.

8. Amino-terminal arginylation targets endoplasmic reticulum chaperone BiP for autophagy through p62 binding.

Review 9. Quality control: ER-associated degradation: protein quality control and beyond.

10. Global analysis of posttranslational protein arginylation.

1. Correlations between Photodegradation of Bisretinoid Constituents of Retina and Dicarbonyl Adduct Deposition.

2. Proteasomal activity-based probes mark protein homeostasis in muscles.

3. Identification of miRNA-eQTLs in maize mature leaf by GWAS.