Literature DB >> 11988749

Taking a bite: proteasomal protein processing.

Michael Rape1, Stefan Jentsch.   

Abstract

The proteasome is a hollow cylindrical protease that contains active sites concealed within its central cavity. Proteasomes usually completely degrade substrates into small peptides, but in a few cases, degradation can yield biologically active protein fragments. Examples of this are the transcription factors NF-kappa B, Spt23p and Mga2p, which are generated from precursors by proteasomal processing. How distinct protein domains are spared from degradation remains a matter of debate. Here, we discuss several models and suggest a novel mechanism for proteasomal processing.

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Year:  2002        PMID： 11988749     DOI： 10.1038/ncb0502-e113

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


  42 in total

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2.  Binding of Substrates to the Central Pore of the Vps4 ATPase Is Autoinhibited by the Microtubule Interacting and Trafficking (MIT) Domain and Activated by MIT Interacting Motifs (MIMs).

Authors:  Han Han; Nicole Monroe; Jörg Votteler; Binita Shakya; Wesley I Sundquist; Christopher P Hill
Journal:  J Biol Chem       Date:  2015-04-01       Impact factor: 5.157

3.  Multisite protein kinase A and glycogen synthase kinase 3beta phosphorylation leads to Gli3 ubiquitination by SCFbetaTrCP.

Authors:  Denis Tempé; Mariana Casas; Sonia Karaz; Marie-Françoise Blanchet-Tournier; Jean-Paul Concordet
Journal:  Mol Cell Biol       Date:  2006-06       Impact factor: 4.272

4.  Further characterization of the signaling proteolysis step in the Aspergillus nidulans pH signal transduction pathway.

Authors:  María M Peñas; América Hervás-Aguilar; Tatiana Múnera-Huertas; Elena Reoyo; Miguel A Peñalva; Herbert N Arst; Joan Tilburn
Journal:  Eukaryot Cell       Date:  2007-04-06

5.  Slippery substrates impair ATP-dependent protease function by slowing unfolding.

Authors:  Daniel A Kraut
Journal:  J Biol Chem       Date:  2013-10-22       Impact factor: 5.157

6.  Proteasomal degradation from internal sites favors partial proteolysis via remote domain stabilization.

Authors:  Daniel A Kraut; Andreas Matouschek
Journal:  ACS Chem Biol       Date:  2011-08-12       Impact factor: 5.100

7.  Gly-Ala repeats induce position- and substrate-specific regulation of 26 S proteasome-dependent partial processing.

Authors:  Chrysoula Daskalogianni; Sébastien Apcher; Marco M Candeias; Nadia Naski; Fabien Calvo; Robin Fåhraeus
Journal:  J Biol Chem       Date:  2008-08-29       Impact factor: 5.157

8.  Site-specific methionine oxidation initiates calmodulin degradation by the 20S proteasome.

Authors:  Edward M Balog; Elizabeth L Lockamy; David D Thomas; Deborah A Ferrington
Journal:  Biochemistry       Date:  2009-04-07       Impact factor: 3.162

9.  The immunoproteasome is induced by cytokines and regulates apoptosis in human islets.

Authors:  Morten Lundh; Marco Bugliani; Tina Dahlby; Danny Hung-Chieh Chou; Bridget Wagner; Seyed Mojtaba Ghiasi; Vincenzo De Tata; Zhifei Chen; Marianne Nissan Lund; Michael J Davies; Piero Marchetti; Thomas Mandrup-Poulsen
Journal:  J Endocrinol       Date:  2017-04-24       Impact factor: 4.286

10.  Proteasomes mediate prolactin-induced receptor down-regulation and fragment generation in breast cancer cells.

Authors:  Juu-Chin Lu; Timothy M Piazza; Linda A Schuler
Journal:  J Biol Chem       Date:  2005-08-15       Impact factor: 5.157
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