Unique Structural Changes in Calcium-Bound Calmodulin Upon Interaction with Protein 4.1R FERM Domain: Novel Insights into the Calcium-dependent Regulation of 4.1R FERM Domain Binding to Membrane Proteins by Calmodulin
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- 作者：Wataru Nunomura (1) (2)
Noriyoshi Isozumi (3)
Shigeyoshi Nakamura (4)
Yuji Jinbo (5)
Shinya Ohki (3)
Shun-ichi Kidokoro (4)
Hideki Wakui (2)
Yuichi Takakuwa (6) - 关键词：Calcium ; bound calmodulin ; Protein 4.1R ; Calorimetry ; NMR
- 刊名：Cell Biochemistry and Biophysics
- 出版年：2014
- 出版时间：May 2014
- 年：2014
- 卷：69
- 期：1
- 页码：7-19
- 全文大小：1,041 KB
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Noriyoshi Isozumi (3)
Shigeyoshi Nakamura (4)
Yuji Jinbo (5)
Shinya Ohki (3)
Shun-ichi Kidokoro (4)
Hideki Wakui (2)
Yuichi Takakuwa (6)
1. Center for Geo-Environmental Science, Graduate School of Engineering and Resource Science, Akita University, Tegata-Gakuên 1-1, Akita, 010-8502, Japan
2. Department of Life Science, Graduate School of Engineering and Resource Science, Akita University, Tegata-Gakuên 1-1, Akita, 010-8502, Japan
3. Center for Nano Materials and Technology, Japan Advanced Institute of Science and Technology, Asahidai 1-1, Nōmi, Ishikawa, 923-1292, Japan
4. Department of Bioengineering, Naga?ka University of Technology, Kamitomi?ka 1603-1, Naga?ka, Niigata, 940-2188, Japan
5. Graduate School of Science and Engineering, Yamagata University, Jyōnan 4-3-16, Yonezawa, Yamagata, 992-8510, Japan
6. Department of Biochemistry, Tokyo Women’s Medical University, Kawada 8-1, Shinjuku, Tokyo, 162-8666, Japan - ISSN：1559-0283
文摘
Calmodulin (CaM) binds to the FERM domain of 80?kDa erythrocyte protein 4.1R (R30) independently of Ca2+ but, paradoxically, regulates R30 binding to transmembrane proteins in a Ca2+-dependent manner. We have previously mapped a Ca2+-independent CaM-binding site, pep11 (A264KKLWKVCVEHHTFFR), in 4.1R FERM domain and demonstrated that CaM, when saturated by Ca2+ (Ca2+/CaM), interacts simultaneously with pep11 and with Ser185 in A181KKLSMYGVDLHKAKD (pep9), the binding affinity of Ca2+/CaM for pep9 increasing dramatically in the presence of pep11. Based on these findings, we hypothesized that pep11 induced key conformational changes in the Ca2+/CaM complex. By differential scanning calorimetry analysis, we established that the C-lobe of CaM was more stable when bound to pep11 either in the presence or absence of Ca2+. Using nuclear magnetic resonance spectroscopy, we identified 8 residues in the N-lobe and 14 residues in the C-lobe of pep11 involved in interaction with CaM in both of presence and absence of Ca2+. Lastly, Kratky plots, generated by small-angle X-ray scattering analysis, indicated that the pep11/Ca2+/CaM complex adopted a relaxed globular shape. We propose that these unique properties may account in part for the previously described Ca2+/CaM-dependent regulation of R30 binding to membrane proteins.