Table 1.

Both Δtailpiece and ΔIQ2 mutations cause defects in localization and assembly

Mutant	Correlation coefficient	Average central myosin
GFP-NMHC-IIA (n = 13)	0.90 ± 0.02	35 ± 4
GFP-NMHC-IIAΔtailpiece (n = 13)	0.93 ± 0.01	18 ± 2*
GFP-NMHC-IIA-S1943A (n = 13)	0.93 ± 0.01	19 ± 2*
GFP-NMHC-IIAΔIQ2 (n = 11)	−0.06 ± 0.10	180 ± 19*

Distribution of transfected GFP-myosin constructs and actin was determined via radial analysis. The correlation coefficient for the resulting GFP-myosin and actin intensity curves was calculated for each cell, and the averages from all cells ± SE are shown. A correlation coefficient of 1 indicates perfect correlation, 0 indicates no correlation, and −1 indicates anti-correlation. Because the GFP-myosin values were normalized to the maximum average intensity, the average central GFP-myosin intensity is a relative measure of lamellar assembly of myosin; lower average central myosin intensity indicates stronger assembly at the lamella, and higher average central myosin intensity indicates weaker assembly at the lamella. GFP-IIAΔtailpiece, GFP-NMHC-IIA-S1943A had significantly stronger assembly at the lamella (Δtailpiece, p = 0.0021; S1943A, p = 0.004). The GFP-IIAΔIQ2 was significantly different from wild type with p = 0.00000007. Asterisks indicate values significantly different from wild type. Significance determined by a two-tailed t test.