کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8325501 | 1539937 | 2010 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Subcellular localisation of the p40phox component of NADPH oxidase involves direct interactions between the Phox homology domain and F-actin
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کلمات کلیدی
Phox homology domainDMEMSDSPAGEGSTDulbecco's modified Eagle's medium - Medal of Eagle اصلاح شده DulbeccoPI(3)P - PI (3) PProtein interaction - تعامل پروتئینPX domain - دامنه PXCell biology - زیست شناسی سلولیsodium dodecyl sulphate - سدیم دودسیل سولفاتphosphatidylinositol-3-phosphate - فسفاتیدیلین سیتول -3 فسفاتPhosphoinositide - فسفوئوزیتیدMALDI-MS - مالدی MSNeutrophils - نوتروفیل هاpolymerase chain reaction - واکنش زنجیره ای پلیمرازPCR - واکنش زنجیرهٔ پلیمرازCytoskeleton - چارچوب یاخته، سیتواسکلتون، اسکلت سلولیpolyacrylamide gelelectrophoresis - ژل الکتروفورز پلی آکریل آمیدglutathione-S-transferase - گلوتاتیون S-ترانسفراز
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Cytosolic components of the NADPH oxidase interact with the actin cytoskeleton. These interactions are thought to be important for the activation of this enzyme system but they are poorly characterised at the molecular level. Here we have explored the interaction between the actin cytoskeleton and p40phox, one of the cytosolic components of NADPH oxidase. Full length p40phox expressed in COS cells co-localised with F-actin in a peripheral lamellar compartment. The co-localisation was lost after deletion of the Phox homology (PX) domain and the PX domain in isolation (p40PX) showed the same F-actin co-localisation as the full length protein. PX domains are known lipid-binding modules however, a mutant p40PX which did not bind lipids still co-localised with F-actin suggesting that lipid-independent interactions underlie the localisation. Affinity chromatography identified actin as a binding partner for p40PX in neutrophil extracts. Pure actin interacted with both p40phox and with p40PX suggesting it is a direct interaction. Disruption of the actin cytoskeleton with cytochalasin D resulted in actin rearrangement and concomitantly the localisation of full length p40phox proteins and that of p40PX changed. Thus p40PX is a dual F-actin/lipid-binding module and F-actin interactions with the PX domain dictate at least in part the intracellular localisation of the cytosolic p40phox subunit of the NADPH oxidase.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: The International Journal of Biochemistry & Cell Biology - Volume 42, Issue 10, October 2010, Pages 1736-1743
Journal: The International Journal of Biochemistry & Cell Biology - Volume 42, Issue 10, October 2010, Pages 1736-1743
نویسندگان
Dongmin Shao, Anthony W. Segal, Lodewijk V. Dekker,