Literature DB >> 19399586

Intracellular protein degradation in mammalian cells: recent developments.

Erwin Knecht1, Carmen Aguado, Jaime Cárcel, Inmaculada Esteban, Juan Miguel Esteve, Ghita Ghislat, José Félix Moruno, José Manuel Vidal, Rosana Sáez.   

Abstract

In higher organisms, dietary proteins are broken down into amino acids within the digestive tract but outside the cells, which incorporate the resulting amino acids into their metabolism. However, under certain conditions, an organism loses more nitrogen than is assimilated in the diet. This additional loss was found in the past century to come from intracellular proteins and started an intensive research that produced an enormous expansion of the field and a dispersed literature. Therefore, our purpose is to provide an updated summary of the current knowledge on the proteolytic machinery involved in intracellular protein degradation and its physiological and pathological relevance, especially addressed to newcomers in the field who may find further details in more specialized reviews. However, even providing a general overview, this is an extremely wide field and, therefore, we mainly focus on mammalian cells, while other cells will be mentioned only for comparison purposes.

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Year:  2009        PMID: 19399586     DOI: 10.1007/s00018-009-0030-6

Source DB:  PubMed          Journal:  Cell Mol Life Sci        ISSN: 1420-682X            Impact factor:   9.261


  85 in total

1.  Two-substrate association with the 20S proteasome at single-molecule level.

Authors:  Silke Hutschenreiter; Ali Tinazli; Kirstin Model; Robert Tampé
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Review 2.  Signalling and autophagy regulation in health, aging and disease.

Authors:  Alfred J Meijer; Patrice Codogno
Journal:  Mol Aspects Med       Date:  2006-09-14

Review 3.  Proteasomes: machines for all reasons.

Authors:  George N Demartino; Thomas G Gillette
Journal:  Cell       Date:  2007-05-18       Impact factor: 41.582

Review 4.  A proteasome for all occasions.

Authors:  John Hanna; Daniel Finley
Journal:  FEBS Lett       Date:  2007-03-30       Impact factor: 4.124

Review 5.  Chaperone-driven proteasome assembly.

Authors:  Rina Rosenzweig; Michael H Glickman
Journal:  Biochem Soc Trans       Date:  2008-10       Impact factor: 5.407

6.  Organization of the pre-autophagosomal structure responsible for autophagosome formation.

Authors:  Tomoko Kawamata; Yoshiaki Kamada; Yukiko Kabeya; Takayuki Sekito; Yoshinori Ohsumi
Journal:  Mol Biol Cell       Date:  2008-02-20       Impact factor: 4.138

7.  JNK1-mediated phosphorylation of Bcl-2 regulates starvation-induced autophagy.

Authors:  Yongjie Wei; Sophie Pattingre; Sangita Sinha; Michael Bassik; Beth Levine
Journal:  Mol Cell       Date:  2008-06-20       Impact factor: 17.970

8.  Trehalose, a novel mTOR-independent autophagy enhancer, accelerates the clearance of mutant huntingtin and alpha-synuclein.

Authors:  Sovan Sarkar; Janet E Davies; Zebo Huang; Alan Tunnacliffe; David C Rubinsztein
Journal:  J Biol Chem       Date:  2006-12-20       Impact factor: 5.157

9.  Control of macroautophagy by calcium, calmodulin-dependent kinase kinase-beta, and Bcl-2.

Authors:  Maria Høyer-Hansen; Lone Bastholm; Piotr Szyniarowski; Michelangelo Campanella; György Szabadkai; Thomas Farkas; Katiuscia Bianchi; Nicole Fehrenbacher; Folmer Elling; Rosario Rizzuto; Ida Stenfeldt Mathiasen; Marja Jäättelä
Journal:  Mol Cell       Date:  2007-01-26       Impact factor: 17.970

Review 10.  The calpains: modular designs and functional diversity.

Authors:  Dorothy E Croall; Klaus Ersfeld
Journal:  Genome Biol       Date:  2007       Impact factor: 13.583

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  32 in total

Review 1.  The role of the ubiquitin-proteasome system in kidney diseases.

Authors:  Hirotaka Fukasawa
Journal:  Clin Exp Nephrol       Date:  2012-06-09       Impact factor: 2.801

Review 2.  Chaperone-mediated autophagy: roles in neuroprotection.

Authors:  Zhibiao Cai; Weijun Zeng; Kai Tao; Zhen E; Bao Wang; Qian Yang
Journal:  Neurosci Bull       Date:  2015-07-23       Impact factor: 5.203

3.  ATP is released from autophagic vesicles to the extracellular space in a VAMP7-dependent manner.

Authors:  Claudio Marcelo Fader; Milton Osmar Aguilera; María Isabel Colombo
Journal:  Autophagy       Date:  2012-09-05       Impact factor: 16.016

4.  Average oxidation state of carbon in proteins.

Authors:  Jeffrey M Dick
Journal:  J R Soc Interface       Date:  2014-11-06       Impact factor: 4.118

5.  Production of an antigenic peptide by insulin-degrading enzyme.

Authors:  Nicolas Parmentier; Vincent Stroobant; Didier Colau; Philippe de Diesbach; Sandra Morel; Jacques Chapiro; Peter van Endert; Benoît J Van den Eynde
Journal:  Nat Immunol       Date:  2010-04-04       Impact factor: 25.606

6.  Intracellular rescue of the uroporphyrinogen III synthase activity in enzymes carrying the hotspot mutation C73R.

Authors:  Arola Fortian; Esperanza González; David Castaño; Juan M Falcon-Perez; Oscar Millet
Journal:  J Biol Chem       Date:  2011-02-22       Impact factor: 5.157

7.  Withdrawal of essential amino acids increases autophagy by a pathway involving Ca2+/calmodulin-dependent kinase kinase-β (CaMKK-β).

Authors:  Ghita Ghislat; Maria Patron; Rosario Rizzuto; Erwin Knecht
Journal:  J Biol Chem       Date:  2012-10-01       Impact factor: 5.157

8.  Mechanisms of autophagy and apoptosis: Recent developments in breast cancer cells.

Authors:  Juan M Esteve; Erwin Knecht
Journal:  World J Biol Chem       Date:  2011-10-26

Review 9.  Biochemical markers of aging for longitudinal studies in humans.

Authors:  Peter M Engelfriet; Eugène H J M Jansen; H Susan J Picavet; Martijn E T Dollé
Journal:  Epidemiol Rev       Date:  2013-02-04       Impact factor: 6.222

10.  Laforin, the most common protein mutated in Lafora disease, regulates autophagy.

Authors:  Carmen Aguado; Sovan Sarkar; Viktor I Korolchuk; Olga Criado; Santiago Vernia; Patricia Boya; Pascual Sanz; Santiago Rodríguez de Córdoba; Erwin Knecht; David C Rubinsztein
Journal:  Hum Mol Genet       Date:  2010-05-07       Impact factor: 6.150

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