Literature DB >> 19468686

Ubiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradation.

Vivian Su1, Alan F Lau.   

Abstract

The ubiquitin-proteasome pathway of protein degradation is one of the major mechanisms that are involved in the maintenance of the proper levels of cellular proteins. The regulation of proteasomal degradation thus ensures proper cell functions. The family of proteins containing ubiquitin-like (UbL) and ubiquitin-associated (UBA) domains has been implicated in proteasomal degradation. UbL-UBA domain containing proteins associate with substrates destined for degradation as well as with subunits of the proteasome, thus regulating the proper turnover of proteins.

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Year:  2009        PMID: 19468686      PMCID: PMC2725189          DOI: 10.1007/s00018-009-0048-9

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


  114 in total

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Review 4.  Sequestosome 1/p62--more than just a scaffold.

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Journal:  FEBS Lett       Date:  2006-12-19       Impact factor: 4.124

5.  Identification and characterization of an ataxin-1-interacting protein: A1Up, a ubiquitin-like nuclear protein.

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Journal:  Hum Mol Genet       Date:  2000-09-22       Impact factor: 6.150

6.  Yeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway.

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Journal:  EMBO J       Date:  2006-11-02       Impact factor: 11.598

7.  Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains.

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Journal:  J Biol Chem       Date:  2003-03-14       Impact factor: 5.157

8.  A novel connexin43-interacting protein, CIP75, which belongs to the UbL-UBA protein family, regulates the turnover of connexin43.

Authors:  Xinli Li; Vivian Su; Wendy E Kurata; Chengshi Jin; Alan F Lau
Journal:  J Biol Chem       Date:  2007-12-13       Impact factor: 5.157

9.  p62 serves as a shuttling factor for TrkA interaction with the proteasome.

Authors:  Thangiah Geetha; M Lamar Seibenhener; Li Chen; Kiran Madura; Marie W Wooten
Journal:  Biochem Biophys Res Commun       Date:  2008-07-01       Impact factor: 3.575

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Journal:  J Cell Biol       Date:  2000-05-29       Impact factor: 10.539

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  61 in total

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Review 2.  Degradation of connexins through the proteasomal, endolysosomal and phagolysosomal pathways.

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Journal:  J Membr Biol       Date:  2012-07-08       Impact factor: 1.843

3.  A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components.

Authors:  Carlos Gorbea; Gregory Pratt; Vicença Ustrell; Russell Bell; Sudhir Sahasrabudhe; Robert E Hughes; Martin Rechsteiner
Journal:  J Biol Chem       Date:  2010-08-03       Impact factor: 5.157

Review 4.  Ubiquitin/proteasome pathway impairment in neurodegeneration: therapeutic implications.

Authors:  Qian Huang; Maria E Figueiredo-Pereira
Journal:  Apoptosis       Date:  2010-11       Impact factor: 4.677

5.  Distribution of the SELMA translocon in secondary plastids of red algal origin and predicted uncoupling of ubiquitin-dependent translocation from degradation.

Authors:  Simone Stork; Daniel Moog; Jude M Przyborski; Ilka Wilhelmi; Stefan Zauner; Uwe G Maier
Journal:  Eukaryot Cell       Date:  2012-10-05

6.  A phylogenetic analysis of the ubiquitin superfamily based on sequence and structural information.

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Review 7.  Connexins: mechanisms regulating protein levels and intercellular communication.

Authors:  Vivian Su; Alan F Lau
Journal:  FEBS Lett       Date:  2014-01-20       Impact factor: 4.124

8.  Degradation of gap junction connexins is regulated by the interaction with Cx43-interacting protein of 75 kDa (CIP75).

Authors:  Jennifer L Kopanic; Barbara Schlingmann; Michael Koval; Alan F Lau; Paul L Sorgen; Vivian F Su
Journal:  Biochem J       Date:  2015-03-15       Impact factor: 3.857

9.  Ubiquilin-mediated Small Molecule Inhibition of Mammalian Target of Rapamycin Complex 1 (mTORC1) Signaling.

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10.  ILRUN, a Human Plasma Lipid GWAS Locus, Regulates Lipoprotein Metabolism in Mice.

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