Table 1. Summary of contribution of... | Rockefeller University Press

Table 1.

Summary of contribution of L223F mutation and N-terminal fusion of a polypeptide from Ci-VSP to enhancement of voltage-dependent enzyme activity of eVSP

	Phosphatase activity (s^-1)	Ratio	n	Phosphatase activity (s^-1)	Ratio	n
	Kir2.1 (on cell)			KCNQ2/3
Dr-VSP WT	1.0 ± 0.8^a	-	17	1.6 ± 1.1^b	-	9
Dr-VSP L223F	1.7 ± 1.2^a	1.7	22	5.5 ± 4.0^b	3.4	9
	Phosphatase activity (s^-1)	Ratio	n	Phosphatase activity(×10² ms)	Ratio	n
	Kir2.1 (whole cell)			TRPC6
Dr-VSP^mChe WT	2.6 ± 2.6^c^,^d^,^e	-	7
Dr-VSP^mChe L223F	4.6 ± 1.6^c^,^f	1.8	8
CiDr-VSP^mChe WT	3.6 ± 2.2^d^,^g	1.4	10	4.1 ± 1.7^h	-	6
CiDr-VSP^mChe L223F	7.3 ± 3.0^e^,^f^,^g	2.8	11	2.0 ± 0.9^h	2.1	3

	Phosphatase activity (s^-1)	Ratio	n	Phosphatase activity (s^-1)	Ratio	n
	Kir2.1 (on cell)			KCNQ2/3
Dr-VSP WT	1.0 ± 0.8^a	-	17	1.6 ± 1.1^b	-	9
Dr-VSP L223F	1.7 ± 1.2^a	1.7	22	5.5 ± 4.0^b	3.4	9
	Phosphatase activity (s^-1)	Ratio	n	Phosphatase activity(×10² ms)	Ratio	n
	Kir2.1 (whole cell)			TRPC6
Dr-VSP^mChe WT	2.6 ± 2.6^c^,^d^,^e	-	7
Dr-VSP^mChe L223F	4.6 ± 1.6^c^,^f	1.8	8
CiDr-VSP^mChe WT	3.6 ± 2.2^d^,^g	1.4	10	4.1 ± 1.7^h	-	6
CiDr-VSP^mChe L223F	7.3 ± 3.0^e^,^f^,^g	2.8	11	2.0 ± 0.9^h	2.1	3

Phosphatase activity is shown as the rate constant (s^-1) or time lag (ms) calculated from inward current decay of Kir2.1 or time-dependent change of TPRC6 current, respectively. Ratio is a comparison between the phosphatase activity of a target and WT. n is sample number. P values were calculated by two-tailed Student’s t test.

P = 0.03.

P = 0.13.

P = 0.46.

P = 0.005.

P = 0.03.

P = 0.007.

P = 0.04.

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