Ubiquitin chains in the Dsk2 UBL domain mediate Dsk2 stability and protein degradation in yeast.

[1]  M. Malaba.  Together , 2012 .

[2]  D. Hoogstraten,et al.  C-terminal UBA domains protect ubiquitin receptors by preventing initiation of protein degradation , 2011, Nature communications.

[3]  K. Hofmann,et al.  The Yeast E4 Ubiquitin Ligase Ufd2 Interacts with the Ubiquitin-like Domains of Rad23 and Dsk2 via a Novel and Distinct Ubiquitin-like Binding Domain* , 2010, The Journal of Biological Chemistry.

[4]  M. Glickman,et al.  Together, Rpn10 and Dsk2 can serve as a polyubiquitin chain-length sensor. , 2009, Molecular cell.

[5]  Vivian F Su,et al.  Ubiquitin-like and ubiquitin-associated domain proteins: significance in proteasomal degradation , 2009, Cellular and Molecular Life Sciences.

[6]  S. Gygi,et al.  Extraproteasomal Rpn10 restricts access of the polyubiquitin-binding protein Dsk2 to proteasome. , 2008, Molecular cell.

[7]  Ivan Dikic,et al.  Proteasome subunit Rpn13 is a novel ubiquitin receptor , 2008, Nature.

[8]  R. Deshaies,et al.  A conditional yeast E1 mutant blocks the ubiquitin-proteasome pathway and reveals a role for ubiquitin conjugates in targeting Rad23 to the proteasome. , 2007, Molecular biology of the cell.

[9]  石井 健士.  Yeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway , 2007 .

[10]  F. Bedford,et al.  The UBL domain of PLIC‐1 regulates aggresome formation , 2006, EMBO reports.

[11]  L. Johnson,et al.  Structures of the Dsk2 UBL and UBA domains and their complex. , 2006, Acta crystallographica. Section D, Biological crystallography.

[12]  J. Endicott,et al.  Budding yeast Dsk2 protein forms a homodimer via its C-terminal UBA domain. , 2005, Biochemical and biophysical research communications.

[13]  S. Elsasser,et al.  Delivery of ubiquitinated substrates to protein-unfolding machines , 2005, Nature Cell Biology.

[14]  D. Fushman,et al.  Diverse polyubiquitin interaction properties of ubiquitin-associated domains , 2005, Nature Structural &Molecular Biology.

[15]  Anna Bakhrat,et al.  The DNA Damage-Inducible UbL-UbA Protein Ddi1 Participates in Mec1-Mediated Degradation of Ho Endonuclease , 2005, Molecular and Cellular Biology.

[16]  M. Masucci,et al.  The UBA2 domain functions as an intrinsic stabilization signal that protects Rad23 from proteasomal degradation. , 2005, Molecular cell.

[17]  R. Deshaies,et al.  Multiubiquitin Chain Receptors Define a Layer of Substrate Selectivity in the Ubiquitin-Proteasome System , 2004, Cell.

[18]  K. Mi,et al.  Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis. , 2004, Molecular biology of the cell.

[19]  D. Finley,et al.  Rad23 and Rpn10 Serve as Alternative Ubiquitin Receptors for the Proteasome* , 2004, Journal of Biological Chemistry.

[20]  P. Howley,et al.  DNA-repair protein hHR23a alters its protein structure upon binding proteasomal subunit S5a , 2003, Proceedings of the National Academy of Sciences of the United States of America.

[21]  G. Dittmar,et al.  Proteasome subunit Rpn1 binds ubiquitin-like protein domains , 2002, Nature Cell Biology.

[22]  Hai Rao,et al.  Recognition of Specific Ubiquitin Conjugates Is Important for the Proteolytic Functions of the Ubiquitin-associated Domain Proteins Dsk2 and Rad23* , 2002, The Journal of Biological Chemistry.

[23]  M. Funakoshi,et al.  Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome , 2002, Proceedings of the National Academy of Sciences of the United States of America.

[24]  Colin Gordon,et al.  Proteins containing the UBA domain are able to bind to multi-ubiquitin chains , 2001, Nature Cell Biology.

[25]  S. Biggins,et al.  Yeast ubiquitin-like genes are involved in duplication of the microtubule organizing center , 1996, The Journal of cell biology.