کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2132208 | 1086679 | 2008 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
p120-catenin is a novel desmoglein 3 interacting partner: Identification of the p120-catenin association site of desmoglein 3
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کلمات کلیدی
FCSRUDp120-cateninDesmogleinsp120ctnDesmosomeNHEKsDSCsICSHEK293DTDDSGkDaDMEMkiloDaltonPBSBSA - BSADulbecco's modified Eagle's medium - Medal of Eagle اصلاح شده Dulbeccobovine serum albumin - آلبومین سرم گاوamino acid - آمینو اسیدSDS-polyacrylamide gel electrophoresis - الکتروفورز ژل SDS-polyacrylamide gelSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدepithelia - اپیتلیاminimal essential medium - حداقل وسایل ضروریextracellular - خارج سلولیdesmoglein - دزوگلینfetal calf serum - سرم گوساله جنینMEM - مامانPhosphate-buffered saline - محلول نمک فسفات با خاصیت بافریhemagglutinin - هماگلوتینینpolymerase chain reaction - واکنش زنجیره ای پلیمرازPCR - واکنش زنجیرهٔ پلیمرازCell adhesion - چسبندگی سلولیCatenin - کاتنینKeratinocyte - کراتینوسیتnormal human epidermal keratinocytes - کراتینوسیت های اپیدرمی طبیعی انسانhuman embryonic kidney 293 - کلیه جنینی انسان 293
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
تحقیقات سرطان
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: p120-catenin is a novel desmoglein 3 interacting partner: Identification of the p120-catenin association site of desmoglein 3 p120-catenin is a novel desmoglein 3 interacting partner: Identification of the p120-catenin association site of desmoglein 3](/preview/png/2132208.png)
چکیده انگلیسی
p120-catenin (p120ctn) is an armadillo-repeat protein that directly binds to the intracytoplasmic domains of classical cadherins. p120ctn binding promotes the stabilization of cadherin complexes on the plasma membrane and thus positively regulates the adhesive activity of cadherins. Using co-immunoprecipitation, we show here that p120ctn associates to desmogleins (Dsg) 1 and 3. To determine which region is involved in the association between Dsg3 and p120ctn, we constructed mutant Dsg3 proteins, in which various cytoplasmic subdomains were removed. The tailless Dsg3 constructs ÎIA:AA1-641Dsg3 and Î641-714Dsg3, which do not contain the intracellular anchor (IA) region, did not coprecipitate with p120cn, nor did they colocalize at the plasma membrane. Immunocytochemical analysis revealed that p120ctn does not localize to desmosomes, but colocalizes with Dsg3 at the cell surface. A biotinylation assay for Dsg3 showed that biotinylated Î641-714Dsg3 was turned over more rapidly than wild-type Dsg3. These results indicate that the membrane proximal region (corresponding to residues 641-714) in the IA region of Dsg3 is necessary for complex formation with p120ctn, and to maintain free Dsg3 at the cell surface before it is integrated into desmosomes. In summary, we show that p120ctn is a novel interactor of the Dsg proteins, and may play a role in desmosome remodeling.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Experimental Cell Research - Volume 314, Issue 8, 1 May 2008, Pages 1683-1692
Journal: Experimental Cell Research - Volume 314, Issue 8, 1 May 2008, Pages 1683-1692
نویسندگان
Miho Kanno, Yasuka Isa, Yumi Aoyama, Yukari Yamamoto, Miki Nagai, Masayuki Ozawa, Yasuo Kitajima,