1. Expression of the polycystin-1 C-terminal cytoplasmic tail increases Cl- channel activity inXenopus oocytes 
Marina N. Chernova, David H. Vandorpe, Jeffrey S. Clark, Seth L. Alper 
Kidney International 
Volume 68, Issue 2, Pages (August 2005)
DOI: /j x
Copyright © 2005 International Society of Nephrology Terms and Conditions

2. Figure 1
Schematic of the CD16.7-PKD1 C-terminal tail fusion proteins studied in this work. CD16.7-PKD1 (1-226) is shown only for reference. Human PKD1 C-terminal tail numbering (1-226) is in bold on the right of each construct, and below the boundaries of the PKD1 fragment in each construct; PKD1 holo-protein amino acid (aa) numbering is below in parentheses. The coiled-coil domain (C-terminal tail aa ) is shaded. Predicted phosphorylation sites are filled circles. Missense disease mutations are marked in and above the uppermost diagram.
(modified from[27])
Kidney International  , DOI: ( /j x)
Copyright © 2005 International Society of Nephrology Terms and Conditions

3. Figure 2
(A)36Cl- uptake induced inXenopus oocytes by the indicated CD16.7-PKD1 constructs or in water-injected oocytes. *P < 0.01 compared to H2O. (B)36Cl- efflux from oocytes expressing CD16.7-PKD1 ( ) is elevated, but that from oocytes expressing CD16.7-PKD1 (1-92) is at the level exhibited by water-injected oocytes. Each symbol connected by lines represents an individual oocyte.
Kidney International  , DOI: ( /j x)
Copyright © 2005 International Society of Nephrology Terms and Conditions

4. Figure 3
(A)36Cl- uptake induced inXenopus oocytes by CD16.7-PKD1 ( ) constructs carrying the indicated disease mutations (Q148P and R199W) or mutations believed to disrupt interactions of the coiled-coil domain (L152P and L152P/A155P). Water-injected oocytes and oocytes expressing CD16.7-PKD1 (1-92) are included as negative controls. (B) The CD16.7-PKD1 ( ) construct encoding the R199W substitution does not exhibit a dominant negative phenotype. Mole ratios of coinjected cRNA are indicated.
Kidney International  , DOI: ( /j x)
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5. Figure 4
Mutations in the putative phosphorylation sites Y160 and S174/S175 lead to loss of36Cl- uptake induced by CD16.7-PKD1 ( ).
Kidney International  , DOI: ( /j x)
Copyright © 2005 International Society of Nephrology Terms and Conditions

6. Figure 5
Effect of PKD2 polypeptide expression. (A) PKD2 polypeptide expression does not confer increased36Cl- uptake onXenopus oocytes, but does attenuate the increased36Cl- uptake induced by expression of CD16.7-PKD1 ( ). (B) PKD2 polypeptide expression does not induce increased current inXenopus oocytes, but does attenuate the increased current associated with expression of CD16.7-PKD1 ( ). (C) PKD2 coexpression severely decreases La3+-sensitive current induced by CD16.7-PKD1 ( ). *P < 0.01.
Kidney International  , DOI: ( /j x)
Copyright © 2005 International Society of Nephrology Terms and Conditions

7. Figure 6
(A)36Cl- efflux from nine oocytes expressing CD16.7-PKD1 ( ) is inhibited by 100 μmol/L NS3623, in contrast to no effect of the drug on two oocytes (top two traces) previously injected with water. Each set of symbols connected by a line represents an individual oocyte. (B) Summary of effects of added NS3623 (100 μmol/L), DIDS (500 μmol/L), and La3+ (1mmol/L) on36Cl- efflux from oocytes expressing CD16.7-PKD1 ( ). Results from assays as in (A) are presented normalized to rate constants in the absence of drug (left bar). (C) Modest inhibition by 100 μmol/L NS3623 of CD16.7-PKD1 ( )-associated whole cell current measured in ND-96 bath. *P < 0.05 (N = 4). (D) Cl- current in representative outside-out patch pulled from oocytes expressing CD16.7-PKD1 ( ) and subjected to a voltage ramp (-120 to +80mV) in NMDG-containing bath before (gray) and 5 minutes after bath exposure to 100 μmol/L NS3623 (black). Inset, NS3623 difference currents at -100mV in oocytes expressing CD16.7-PKD ( ) and in oocytes previously injected with water (N = 4). *P = 0.02.
Kidney International  , DOI: ( /j x)
Copyright © 2005 International Society of Nephrology Terms and Conditions