Correction
for
Jones et al., J. Gen. Physiol. 112 (2) 125-143.
© The Rockefeller University Press, 0022-1295/1998//523/ $5.00
Journal of General Physiology, Volume 112, Number 4, 1998
Correction
Jones, L.P., S.-k. Wei, and D.T. Yue. The Journal of General Physiology. Volume 112, No. 2, August 1998. 125–143.
Page 137.
Line five of Figure 9 legend contained an error in which two symbols were incorrectly labelled. The correct legend is shown below.
FIGURE 9. Activation and inactivation properties of a COOH-terminal truncated version of 
1E (1E
, amino acids 1–1871) that lacks a putative β binding site. All measurements for both 1E and 1E are in 10 mM Ba2+. (A) Traces illustrating activation of ionic currents for 1E2
(cell 375_19) or 1Eβ2a2 (cell 370_6) using the same voltage protocol as in Fig. 2. Data are shown for test pulse potentials of –30, –20, –10, 10, and 50 mV. (B) Comparison of G-V for 1E and 1E indicates that modulation of 1E activation by β subunits is preserved. Symbols correspond to data for 1E and wild-type 1E (1Eβ2a2, 
, n = 4; 1E2, •, n = 11; 1E2, 
, n = 11; and 1Eβ2a, 
, n = 8). Lines are single-Boltzmann fits to the 1E2 and 1Eβ2a data with fit parameters z = 2.4, V1/2 = –10.1; and z = 3.4, V1/2 = –18.2, respectively. The shift in V1/2 values relative to Fig. 6 C corresponds to a surface potential shift between 10 mM (used here) and 2 mM Ba2+ (Fig. 6). (C) Steady state inactivation. Traces after a 20-s prepulse (as in Fig. 7) to the indicated potentials are shown for 1E in combination with 2 (cell 376_9), β3 (cell 375_4), β2a2 (cell 370_11), and β32 (cell 371_10). (D) Comparison of h(
)-V relations for 1E (symbols) and 1E (same data as in Fig. 7, shown as lines connecting mean data values, without explicit reproduction of data points as symbols). Symbols correspond to the following constructs: 1E2, •; 1Eβ2a2, ; 1Eβ3, 
; 1Eβ32, x. Data for 1E is shifted by –7 mV to overlay the 1E data. Average fit values and cell numbers are summarized in Tables V (G-V) and III [h()-V] for both 1E and 1E.
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