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Table 2 The interaction of wild type and mutant profilins with α-actin.

From: Mutational analysis of human profilin I reveals a second PI(4,5)-P2 binding site neighbouring the poly(L-proline) binding site

 

K d (μM)

% F-actin at T 1/2

Actin

-

50

Human profilin I

0.35

12

R74A

N.B.

35

R74E

N.B.

69

R88A

1.4

23

S56E

0.36

19

R135D

0.4

18

R136D

0.23

16

S56E/R74E

N.B.

56

S56E/R74A

N.B.

41

S56E/R88E

N.B.

43

R74E/R88E

N.B.

47

R135A/R136A

0.41

14

R88A/R136D

7.9

57

R88E/R136D

6.6

76

W3A

0.33

N.T.

Rat profilin IIa

0.38

N.T.

W3A

0.18

N.T.

Profilin IIa-myc

0.13

N.T.

  1. The Kd-values were determined using capped filament ends, 5% pyrene labeled actin and 1.5 μM profilin. % F-actin at T1/2 is representative for the activity of the profilin mutants during actin polymerization and is derived from curves as in Figure 4. T1/2 is the time point where actin alone reaches 50% polymerization. The values in this table are averages of three to five different measurements. N.B. indicates no binding and N.T. is not tested.
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BMC Biochemistry

ISSN: 1471-2091

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