NDLI: 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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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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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

Content Provider	Springer Nature Link
Author	Numura, Wataru Isozumi, riyoshi Nakamura, Shigeyoshi Jinbo, Yuji Ohki, Shinya Kidokoro, Shun ichi Wakui, Hideki Takakuwa, Yuichi
Copyright Year	2013
Abstract	Calmodulin (CaM) binds to the FERM domain of 80 kDa erythrocyte protein 4.1R (R30) independently of Ca$^{2+}$ but, paradoxically, regulates R30 binding to transmembrane proteins in a Ca$^{2+}$-dependent manner. We have previously mapped a Ca$^{2+}$-independent CaM-binding site, pep11 (A$^{264}$KKLWKVCVEHHTFFR), in 4.1R FERM domain and demonstrated that CaM, when saturated by Ca$^{2+}$ (Ca$^{2+}$/CaM), interacts simultaneously with pep11 and with Ser$^{185}$ in A$^{181}$KKLSMYGVDLHKAKD (pep9), the binding affinity of Ca$^{2+}$/CaM for pep9 increasing dramatically in the presence of pep11. Based on these findings, we hypothesized that pep11 induced key conformational changes in the Ca$^{2+}$/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 Ca$^{2+}$. 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 Ca$^{2+}$. Lastly, Kratky plots, generated by small-angle X-ray scattering analysis, indicated that the pep11/Ca$^{2+}$/CaM complex adopted a relaxed globular shape. We propose that these unique properties may account in part for the previously described Ca$^{2+}$/CaM-dependent regulation of R30 binding to membrane proteins.
Starting Page	7
Ending Page	19
Page Count	13
File Format	PDF
ISSN	10859195
Journal	Cell Biochemistry and Biophysics
Volume Number	69
Issue Number	1
e-ISSN	15590283
Language	English
Publisher	Springer US
Publisher Date	2013-10-01
Publisher Place	Boston
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Calcium-bound calmodulin Protein 4.1R Calorimetry NMR Biochemistry Pharmacology/Toxicology Biotechnology Cell Biology Biophysics and Biological Physics
Content Type	Text
Resource Type	Article
Subject	Cell Biology Medicine Biochemistry Biophysics

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