کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10768291 | 1050806 | 2005 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Role of interaction with vinculin in recruitment of vinexins to focal adhesions
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Although vinexin was originally identified as a protein binding to the proline-rich hinge region of vinculin, the functions and biochemical properties of the vinexin-vinculin interaction are not known. Here, we determined the affinity of the vinexin-vinculin interaction using surface plasmon resonance measurements and found that vinexin β interacts with the C-terminal half of vinculin, which mimics an activated “open” form, with a threefold higher affinity than with the full-length “closed” vinculin. Coimmunoprecipitation experiments showed that cell adhesion on fibronectin enhances the vinexin-vinculin interaction. We also show that the interaction with vinculin is necessary for the efficient localization of vinexin α and β at focal adhesions. These observations suggest a model that “activated” vinculin localized at focal adhesions recruits vinexins to focal adhesions.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 336, Issue 1, 14 October 2005, Pages 239-246
Journal: Biochemical and Biophysical Research Communications - Volume 336, Issue 1, 14 October 2005, Pages 239-246
نویسندگان
Honami Takahashi, Masaru Mitsushima, Naoya Okada, Takuya Ito, Sanae Aizawa, Rie Akahane, Tsutomu Umemoto, Kazumitsu Ueda, Noriyuki Kioka,