کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5506236 | 1400289 | 2017 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
A pleckstrin homology-like domain is critical for F-actin binding and cofilin-phosphatase activity of Slingshot-1
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
CFPSSHp-cofilinPleckstrin homology (PH) domainITKSlingshotOSBPBtk - BTKactin binding - اتصال آکتینBruton's tyrosine kinase - تیروزین کیناز Brutoncircular dichroism - رنگ تابی دورانیPhosphatase - فسفاتازwild-type - نوع وحشیPleckstrin Homology - همخوانی PleckstrinOxysterol-binding protein - پروتئین اتصال دهنده اکسسترینcyan fluorescent protein - پروتئین فلورسنت سیانوژنCofilin - کوفیلین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Slingshot-1 (SSH1) is a protein phosphatase that specifically dephosphorylates and activates cofilin, an F-actin-severing protein. SSH1 binds to and co-localizes with F-actin, and the cofilin-phosphatase activity of SSH1 is markedly increased by binding to F-actin. In this study, we performed a secondary structure analysis of SSH1, which predicted the existence of a pleckstrin homology (PH)-like domain in the N-terminal region of SSH1. SSH1 also contains a DEK-C domain in the N-terminal region. The N-terminal fragment of SSH1 bound to and co-localized with F-actin, but mutation at Arg-96 or a Leu-His-Lys (LHK) motif in the PH-like domain reduced this activity. Furthermore, mutation at Arg-96 abrogated the cofilin-phosphatase activity of SSH1 in the presence of F-actin. These results suggest that the N-terminal PH-like domain plays a critical role in F-actin binding and F-actin-mediated activation of the cofilin-phosphatase activity of SSH1.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 482, Issue 4, 22 January 2017, Pages 686-692
Journal: Biochemical and Biophysical Research Communications - Volume 482, Issue 4, 22 January 2017, Pages 686-692
نویسندگان
Katsunori Takahashi, Haruka Okabe, Shin-ichiro Kanno, Tomoaki Nagai, Kensaku Mizuno,