دورية أكاديمية
Cdc50p plays a vital role in the ATPase reaction cycle of the putative aminophospholipid transporter Drs2p.
| العنوان: | Cdc50p plays a vital role in the ATPase reaction cycle of the putative aminophospholipid transporter Drs2p. |
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| المؤلفون: | Lenoir G; Department of Membrane Enzymology, Bijvoet Center and Institute of Biomembranes, Utrecht University, 3584 CH Utrecht, The Netherlands., Williamson P, Puts CF, Holthuis JC |
| المصدر: | The Journal of biological chemistry [J Biol Chem] 2009 Jul 03; Vol. 284 (27), pp. 17956-67. Date of Electronic Publication: 2009 May 02. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology |
| مواضيع طبية MeSH: | Adenosine Triphosphatases/*metabolism , Calcium-Transporting ATPases/*metabolism , Saccharomyces cerevisiae/*enzymology , Saccharomyces cerevisiae Proteins/*metabolism, Adenosine Triphosphatases/genetics ; Adenosine Triphosphate/metabolism ; Calcium-Transporting ATPases/genetics ; Catalysis ; Catalytic Domain/physiology ; In Vitro Techniques ; Multiprotein Complexes/metabolism ; Mutagenesis ; Phosphorylation/physiology ; Protein Subunits/genetics ; Protein Subunits/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae Proteins/genetics ; Transfection ; Ubiquitin/metabolism |
| مستخلص: | Members of the P(4) subfamily of P-type ATPases are believed to catalyze transport of phospholipids across cellular bilayers. However, most P-type ATPases pump small cations or metal ions, and atomic structures revealed a transport mechanism that is conserved throughout the family. Hence, a challenging problem is to understand how this mechanism is adapted in P(4)-ATPases to flip phospholipids. P(4)-ATPases form heteromeric complexes with Cdc50 proteins. The primary role of these additional polypeptides is unknown. Here, we show that the affinity of yeast P(4)-ATPase Drs2p for its Cdc50-binding partner fluctuates during the transport cycle, with the strongest interaction occurring at a point where the enzyme is loaded with phospholipid ligand. We also find that specific interactions with Cdc50p are required to render the ATPase competent for phosphorylation at the catalytically important aspartate residue. Our data indicate that Cdc50 proteins are integral components of the P(4)-ATPase transport machinery. Thus, acquisition of these subunits may have been a crucial step in the evolution of flippases from a family of cation pumps. |
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| المشرفين على المادة: | 0 (CDC50 protein, S cerevisiae) 0 (DRS2 protein, S cerevisiae) 0 (Multiprotein Complexes) 0 (Protein Subunits) 0 (Saccharomyces cerevisiae Proteins) 0 (Ubiquitin) 8L70Q75FXE (Adenosine Triphosphate) EC 3.6.1.- (Adenosine Triphosphatases) EC 7.2.2.10 (Calcium-Transporting ATPases) |
| تواريخ الأحداث: | Date Created: 20090505 Date Completed: 20091027 Latest Revision: 20240322 |
| رمز التحديث: | 20240322 |
| مُعرف محوري في PubMed: | PMC2709398 |
| DOI: | 10.1074/jbc.M109.013722 |
| PMID: | 19411703 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 1083-351X |
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| DOI: | 10.1074/jbc.M109.013722 |