Assembly of the 26S proteasome is regulated by phosphorylation of the p45/Rpt6 ATPase subunit. 2001

K Satoh, and H Sasajima, and K I Nyoumura, and H Yokosawa, and H Sawada
Department of Biochemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan.

We investigated whether the assembly/disassembly of the 26S proteasome is regulated by phosphorylation/dephosphorylation. The regulatory complex disassembled from the 26S proteasome was capable of phosphorylating the p45/Sug1/Rpt6 subunit, suggesting that the protein kinase is activated upon dissociation of the 26S proteasome or that the phosphorylation site of p45 becomes susceptible to the protein kinase. In addition, the p45-phosphorylated regulatory complex was found to be incorporated into the 26S proteasome. When the 26S proteasome was treated with alkaline phosphatase, it was dissociated into the 20S proteasome and the regulatory complex. Furthermore, the p45 subunit and the C3/alpha2 subunit were cross-linked with DTBP, whereas these subunits were not cross-linked by dephosphorylating the 26S proteasome. These results indicate that the 26S proteasome is disassembled into the constituent subcomplexes by dephosphorylation and that it is assembled by phosphorylation of p45 by a protein kinase, which is tightly associated with the regulatory complex. It was also revealed that the p45 subunit is directly associated with the 20S proteasome alpha-subunit C3 in a phosphorylation-dependent manner.

UI MeSH Term Description Entries
D007096 Imidoesters Esters of the hypothetical imidic acids. They react with amines or amino acids to form amidines and are therefore used to modify protein structures and as cross-linking agents. Imidates
D009097 Multienzyme Complexes Systems of enzymes which function sequentially by catalyzing consecutive reactions linked by common metabolic intermediates. They may involve simply a transfer of water molecules or hydrogen atoms and may be associated with large supramolecular structures such as MITOCHONDRIA or RIBOSOMES. Complexes, Multienzyme
D010447 Peptide Hydrolases Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES. Peptidase,Peptidases,Peptide Hydrolase,Protease,Proteases,Proteinase,Proteinases,Proteolytic Enzyme,Proteolytic Enzymes,Esteroproteases,Enzyme, Proteolytic,Hydrolase, Peptide
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D011494 Protein Kinases A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein. Protein Kinase,Kinase, Protein,Kinases, Protein
D002352 Carrier Proteins Proteins that bind or transport specific substances in the blood, within the cell, or across cell membranes. Binding Proteins,Carrier Protein,Transport Protein,Transport Proteins,Binding Protein,Protein, Carrier,Proteins, Carrier
D003432 Cross-Linking Reagents Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other. Bifunctional Reagent,Bifunctional Reagents,Cross Linking Reagent,Crosslinking Reagent,Cross Linking Reagents,Crosslinking Reagents,Linking Reagent, Cross,Linking Reagents, Cross,Reagent, Bifunctional,Reagent, Cross Linking,Reagent, Crosslinking,Reagents, Bifunctional,Reagents, Cross Linking,Reagents, Cross-Linking,Reagents, Crosslinking
D003546 Cysteine Endopeptidases ENDOPEPTIDASES which have a cysteine involved in the catalytic process. This group of enzymes is inactivated by CYSTEINE PROTEINASE INHIBITORS such as CYSTATINS and SULFHYDRYL REAGENTS.
D004591 Electrophoresis, Polyacrylamide Gel Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D000074183 ATPases Associated with Diverse Cellular Activities A large highly conserved family of ATPases with diverse functions in cells that are characterized by the presence of a P-LOOP and a ring shape. They couple the energy generated by ATP hydrolysis to remodeling or mechanical translocation of their target molecules. AAA ATPase,AAA Protease,AAA+ ATPase,AAA+ Protease,AAA ATPases,AAA Proteases,AAA+ ATPases,AAA+ Proteases,ATPase, AAA,ATPase, AAA+,ATPases, AAA+,Protease, AAA,Protease, AAA+,Proteases, AAA,Proteases, AAA+

Related Publications

K Satoh, and H Sasajima, and K I Nyoumura, and H Yokosawa, and H Sawada
June 2007, The FEBS journal,
K Satoh, and H Sasajima, and K I Nyoumura, and H Yokosawa, and H Sawada
August 2007, The Journal of biological chemistry,
K Satoh, and H Sasajima, and K I Nyoumura, and H Yokosawa, and H Sawada
July 1998, FEBS letters,
K Satoh, and H Sasajima, and K I Nyoumura, and H Yokosawa, and H Sawada
May 2013, Structure (London, England : 1993),
K Satoh, and H Sasajima, and K I Nyoumura, and H Yokosawa, and H Sawada
January 1999, Biochemical and biophysical research communications,
K Satoh, and H Sasajima, and K I Nyoumura, and H Yokosawa, and H Sawada
April 1995, FEBS letters,
K Satoh, and H Sasajima, and K I Nyoumura, and H Yokosawa, and H Sawada
January 2020, Proceedings of the National Academy of Sciences of the United States of America,
K Satoh, and H Sasajima, and K I Nyoumura, and H Yokosawa, and H Sawada
January 2021, eNeuro,
K Satoh, and H Sasajima, and K I Nyoumura, and H Yokosawa, and H Sawada
June 2007, Journal of neurochemistry,
K Satoh, and H Sasajima, and K I Nyoumura, and H Yokosawa, and H Sawada
April 2017, Protein & cell,
Copied contents to your clipboard!