کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1948591 | 1054702 | 2007 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Interaction of receptor-activity-modifying protein1 with tubulin Interaction of receptor-activity-modifying protein1 with tubulin](/preview/png/1948591.png)
Receptor-activity-modifying protein (RAMP) 1 is an accessory protein of the G protein-coupled calcitonin receptor-like receptor (CLR). The CLR/RAMP1 heterodimer defines a receptor for the potent vasodilatory calcitonin gene-related peptide. A wider tissue distribution of RAMP1, as compared to that of the CLR, is consistent with additional biological functions. Here, glutathione S-transferase (GST) pull-down, coimmunoprecipitation and yeast two-hybrid experiments identified β-tubulin as a novel RAMP1-interacting protein. GST pull-down experiments indicated interactions between the N- and C-terminal domains of RAMP1 and β-tubulin. Yeast two-hybrid experiments confirmed the interaction between the N-terminal region of RAMP1 and β-tubulin. Interestingly, α-tubulin was co-extracted with β-tubulin in pull-down experiments and immunoprecipitation of RAMP1 coprecipitated α- and β-tubulin. Confocal microscopy indicated colocalization of RAMP1 and tubulin predominantly in axon-like processes of neuronal differentiated human SH-SY5Y neuroblastoma cells. In conclusion, the findings point to biological roles of RAMP1 beyond its established interaction with G protein-coupled receptors.
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1770, Issue 8, August 2007, Pages 1145–1150