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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Ye, Yihong Meyer, Hemmo H. Rapoport, Tom A. |
| Description | Author Affiliation: Ye Y ( Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA.) |
| Abstract | Amember of the family of ATPases associated with diverse cellular activities, called p97 in mammals and Cdc48 in yeast, associates with the cofactor Ufd1–Npl4 to move polyubiquitinated polypeptides from the endoplasmic reticulum (ER) membrane into the cytosol for their subsequent degradation by the proteasome. Here, we have studied the mechanism by which the p97–Ufd1–Npl4 complex functions in this retrotranslocation pathway. Substrate binding occurs when the first ATPase domain of p97 (D1 domain) is in its nucleotide-bound state, an interaction that also requires an association of p97 with the membrane through its $NH_{2}-terminal$ domain. The two ATPase domains (D1 and D2) of p97 appear to alternate in ATP hydrolysis, which is essential for the movement of polypeptides from the ER membrane into the cytosol. The ATPase itself can interact with nonmodified polypeptide substrates as they emerge from the ER membrane. Polyubiquitin chains linked by lysine 48 are recognized in a synergistic manner by both p97 and an evolutionarily conserved ubiquitin-binding site at the $NH_{2}$ terminus of Ufd1. We propose a dual recognition model in which the ATPase complex binds both a nonmodified segment of the substrate and the attached polyubiquitin chain; polyubiquitin binding may activate the ATPase p97 to pull the polypeptide substrate out of the membrane. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 1 |
| Volume Number | 162 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 2003-07-07 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Adenosine Triphosphatases Metabolism Cytosol Enzymology Endoplasmic Reticulum Eukaryotic Cells Nuclear Pore Complex Proteins Nuclear Proteins Protein Transport Genetics Saccharomyces Cerevisiae Proteins Yeasts Adenosine Triphosphate Cells, Cultured Cysteine Endopeptidases Ultrastructure Cytology Intracellular Membranes Lysine Models, Molecular Multienzyme Complexes Mutation Nucleocytoplasmic Transport Proteins Peptides Proteasome Endopeptidase Complex Protein Binding Physiology Protein Structure, Tertiary Ubiquitin Vesicular Transport Proteins Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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