NDLI: Oligomerization of the Polycystin-2 C-terminal Tail and Effects on Its $Ca^{2+}-binding$ $Properties^{*}$

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Oligomerization of the Polycystin-2 C-terminal Tail and Effects on Its $Ca^{2+}-binding$ $Properties^{*}$

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Lolis, Elias J. Keeler, Camille Yang, Yifei Hodsdon, Michael E. Kuo, Ivana Y. Ehrlich, Barbara E.
Description	Author Affiliation: Yang Y ( From the Departments of Laboratory Medicine, Pharmacology, and yifei.yang@yale.edu.); Keeler C ( From the Departments of Laboratory Medicine.); Kuo IY ( Pharmacology, and.); Lolis EJ ( Pharmacology, and.); Ehrlich BE ( Pharmacology, and Cellular and Molecular Physiology, School of Medicine, Yale University, New Haven, Connecticut 06520.); Hodsdon ME ( From the Departments of Laboratory Medicine, michael.hodsdon@yale.edu.)
Abstract	Polycystin-2 (PC2) belongs to the transient receptor potential (TRP) family and forms a $Ca^{2+}-regulated$ channel. The C-terminal cytoplasmic tail of human PC2 (HPC2 Cterm) is important for PC2 channel assembly and regulation. In this study, we characterized the oligomeric states and $Ca^{2+}-binding$ profiles in the C-terminal tail using biophysical approaches. Specifically, we determined that HPC2 Cterm forms a trimer in solution with and without $Ca^{2+}$ bound, although TRP channels are believed to be tetramers. We found that there is only one $Ca^{2+}-binding$ site in the HPC2 Cterm, located within its EF-hand domain. However, the $Ca^{2+}$ binding affinity of the HPC2 Cterm trimer is greatly enhanced relative to the intrinsic binding affinity of the isolated EF-hand domain. We also employed the sea urchin PC2 (SUPC2) as a model for biophysical and structural characterization. The sea urchin C-terminal construct (SUPC2 Ccore) also forms trimers in solution, independent of $Ca^{2+}$ binding. In contrast to the human PC2, the SUPC2 Ccore contains two cooperative $Ca^{2+}-binding$ sites within its EF-hand domain. Consequently, trimerization does not further improve the affinity of $Ca^{2+}$ binding in the SUPC2 Ccore relative to the isolated EF-hand domain. Using NMR, we localized the $Ca^{2+}-binding$ sites in the SUPC2 Ccore and characterized the conformational changes in its EF-hand domain due to trimer formation. Our study provides a structural basis for understanding the $Ca^{2+}-dependent$ regulation of the PC2 channel by its cytosolic C-terminal domain. The improved methodology also serves as a good strategy to characterize other $Ca^{2+}-binding$ proteins.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	16
Volume Number	290
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2015-04-17
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Calcium Metabolism Sea Urchins TRPP Cation Channels Chemistry Amino Acid Sequence Animals Binding Sites Ion Channel Gating Ion Transport Models, Molecular Molecular Sequence Data Protein Aggregates Protein Binding Protein Isoforms Genetics Protein Multimerization Protein Structure, Secondary Protein Structure, Tertiary Recombinant Proteins Sequence Alignment Species Specificity Thermodynamics Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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