Bid is subject to posttranslational modifications within the loop between α helix 2 and α helix 3 (amino acids 39 81 in the mouse protein; Figure 2A).
The Thr649Ala mutation did not alter the insulin-stimulated phosphorylations of five other sites on AS160, namely Ser325, Ser348, Ser577, Ser595, and Ser758 (residue numbers for the mouse protein; Figure 2 and Figure S2A) in the skeletal and cardiac muscle extracts derived from AS160 knockin animals.
Close examination of the C-terminal tail of human NOXO1 reveals a region comprising a number of basic residues that is absent in the mouse protein (see Figure 1B) (residues 347 359, ERRPRRQGRPRG).
As suggested by Reviewer 1, we have also included additional results obtained with our recombinant mouse Protein S, in Figure 2, panels B, E and Figure 2-figure supplement 1.
We screened a series of antibodies to identify appropriate antibodies, which detected bovine and mouse proteins (Supplementary Figure S2A).
However, the lysozyme c-1 antibody (9122) did not cross-react with any mouse serum proteins (Figure 1F, lane MB) nor did it bind to ookinetes cultured from mouse blood (results were similar to absence of texas-red signal as presented in Figure 2, upper left panel).
Somewhat surprisingly, levels of IL-4 in granulomas from SOM−/− mice (1,084 ± 130 pg/mg total protein; Figure 3(b)) were increased compared to levels in granulomas from WT mice (568 ± 97 pg/mg; P < 0.05).
The nature of this diversity was also illustrated using the same workflow implemented on target proteins that are also hubs in the mouse protein interaction network (as depicted in Figure 2(b)).
Levels of IFN- γ in the granulomas derived from SOM−/− mice (219 ± 32 pg/mg total protein; Figure 3(a)) were increased 1.5-fold relative to levels in granulomas of WT mice (142 ± 21 pg/mg; P < 0.05); however, levels of IL-2 in granulomas of SOM−/− mice (548 ± 91 pg/mg total protein) were not different from levels in granulomas of WT mice (714 ± 255 pg/mg; P > 0.05).
Notably, mice without Baicalin treatment developed severe nephritis with increased urine protein, while mice receiving Baicalin were protected against nephritis with decreased urine protein (Figure 4A-C).
The RBM44 mRNAs encode 1013 aa and 1052 aa proteins in mouse and human, respectively (Figure 7C and D), and these human and mouse proteins are highly conserved (Figure 7C).
