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Matches in Nanopublications for { ?s ?p "To investigate whether this partially active Akt is functional in vivo, we first examined the in vivo phosphorylation of GSK3. Surprisingly, phosphorylation of GSK3a at Ser21 and GSK3b at Ser9 in response to serum or insulin was only marginally affected in the SIN1-/- cells (Figure 3C). We also did not observe a difference in the kinetics of GSK3 phosphorylation between the wild-type and SIN1-/- cells (data not shown). These results suggest that the singly Thr308-phosphorylated form of Akt may be partially functional in vivo. We also examined phosphorylation of TSC2, another Akt target (Manning et al., 2002), at the Akt target sites Ser939 and Thr1462 and found no significant difference between wild-type and SIN1-/- cells upon serum and insulin stimulation (Figure 3C). Furthermore, we compared the proliferation rates of several sets of MEFs with wildtype, SIN1+/-, and SIN1-/- genotypes established from E10 embryos. No significant difference in the cell-doubling time of these MEFs was observed (Figure 3D). Finally, we did not find any size difference of wild-type and SIN1-/- cells grown under starvation or normal growth conditions (Figure 3E and data not shown). Hence, the growth factorinduced GSK3 and TSC2 phosphorylation may not fully depend on Akt-Ser473 phosphorylation. Phosphorylation at Thr24/Thr32 of FoxO1/FoxO3a, an Akt Target for the Cell-Survival Pathway, Is Defective in SIN1-/- Cells" ?g. }

• _7 value "To investigate whether this partially active Akt is functional in vivo, we first examined the in vivo phosphorylation of GSK3. Surprisingly, phosphorylation of GSK3a at Ser21 and GSK3b at Ser9 in response to serum or insulin was only marginally affected in the SIN1-/- cells (Figure 3C). We also did not observe a difference in the kinetics of GSK3 phosphorylation between the wild-type and SIN1-/- cells (data not shown). These results suggest that the singly Thr308-phosphorylated form of Akt may be partially functional in vivo. We also examined phosphorylation of TSC2, another Akt target (Manning et al., 2002), at the Akt target sites Ser939 and Thr1462 and found no significant difference between wild-type and SIN1-/- cells upon serum and insulin stimulation (Figure 3C). Furthermore, we compared the proliferation rates of several sets of MEFs with wildtype, SIN1+/-, and SIN1-/- genotypes established from E10 embryos. No significant difference in the cell-doubling time of these MEFs was observed (Figure 3D). Finally, we did not find any size difference of wild-type and SIN1-/- cells grown under starvation or normal growth conditions (Figure 3E and data not shown). Hence, the growth factorinduced GSK3 and TSC2 phosphorylation may not fully depend on Akt-Ser473 phosphorylation. Phosphorylation at Thr24/Thr32 of FoxO1/FoxO3a, an Akt Target for the Cell-Survival Pathway, Is Defective in SIN1-/- Cells" provenance.
• _11 value "To investigate whether this partially active Akt is functional in vivo, we first examined the in vivo phosphorylation of GSK3. Surprisingly, phosphorylation of GSK3a at Ser21 and GSK3b at Ser9 in response to serum or insulin was only marginally affected in the SIN1-/- cells (Figure 3C). We also did not observe a difference in the kinetics of GSK3 phosphorylation between the wild-type and SIN1-/- cells (data not shown). These results suggest that the singly Thr308-phosphorylated form of Akt may be partially functional in vivo. We also examined phosphorylation of TSC2, another Akt target (Manning et al., 2002), at the Akt target sites Ser939 and Thr1462 and found no significant difference between wild-type and SIN1-/- cells upon serum and insulin stimulation (Figure 3C). Furthermore, we compared the proliferation rates of several sets of MEFs with wildtype, SIN1+/-, and SIN1-/- genotypes established from E10 embryos. No significant difference in the cell-doubling time of these MEFs was observed (Figure 3D). Finally, we did not find any size difference of wild-type and SIN1-/- cells grown under starvation or normal growth conditions (Figure 3E and data not shown). Hence, the growth factorinduced GSK3 and TSC2 phosphorylation may not fully depend on Akt-Ser473 phosphorylation. Phosphorylation at Thr24/Thr32 of FoxO1/FoxO3a, an Akt Target for the Cell-Survival Pathway, Is Defective in SIN1-/- Cells" provenance.
• _5 value "To investigate whether this partially active Akt is functional in vivo, we first examined the in vivo phosphorylation of GSK3. Surprisingly, phosphorylation of GSK3a at Ser21 and GSK3b at Ser9 in response to serum or insulin was only marginally affected in the SIN1-/- cells (Figure 3C). We also did not observe a difference in the kinetics of GSK3 phosphorylation between the wild-type and SIN1-/- cells (data not shown). These results suggest that the singly Thr308-phosphorylated form of Akt may be partially functional in vivo. We also examined phosphorylation of TSC2, another Akt target (Manning et al., 2002), at the Akt target sites Ser939 and Thr1462 and found no significant difference between wild-type and SIN1-/- cells upon serum and insulin stimulation (Figure 3C). Furthermore, we compared the proliferation rates of several sets of MEFs with wildtype, SIN1+/-, and SIN1-/- genotypes established from E10 embryos. No significant difference in the cell-doubling time of these MEFs was observed (Figure 3D). Finally, we did not find any size difference of wild-type and SIN1-/- cells grown under starvation or normal growth conditions (Figure 3E and data not shown). Hence, the growth factorinduced GSK3 and TSC2 phosphorylation may not fully depend on Akt-Ser473 phosphorylation. Phosphorylation at Thr24/Thr32 of FoxO1/FoxO3a, an Akt Target for the Cell-Survival Pathway, Is Defective in SIN1-/- Cells" provenance.
• _7 value "To investigate whether this partially active Akt is functional in vivo, we first examined the in vivo phosphorylation of GSK3. Surprisingly, phosphorylation of GSK3a at Ser21 and GSK3b at Ser9 in response to serum or insulin was only marginally affected in the SIN1-/- cells (Figure 3C). We also did not observe a difference in the kinetics of GSK3 phosphorylation between the wild-type and SIN1-/- cells (data not shown). These results suggest that the singly Thr308-phosphorylated form of Akt may be partially functional in vivo. We also examined phosphorylation of TSC2, another Akt target (Manning et al., 2002), at the Akt target sites Ser939 and Thr1462 and found no significant difference between wild-type and SIN1-/- cells upon serum and insulin stimulation (Figure 3C). Furthermore, we compared the proliferation rates of several sets of MEFs with wildtype, SIN1+/-, and SIN1-/- genotypes established from E10 embryos. No significant difference in the cell-doubling time of these MEFs was observed (Figure 3D). Finally, we did not find any size difference of wild-type and SIN1-/- cells grown under starvation or normal growth conditions (Figure 3E and data not shown). Hence, the growth factorinduced GSK3 and TSC2 phosphorylation may not fully depend on Akt-Ser473 phosphorylation. Phosphorylation at Thr24/Thr32 of FoxO1/FoxO3a, an Akt Target for the Cell-Survival Pathway, Is Defective in SIN1-/- Cells" provenance.
• _11 value "To investigate whether this partially active Akt is functional in vivo, we first examined the in vivo phosphorylation of GSK3. Surprisingly, phosphorylation of GSK3a at Ser21 and GSK3b at Ser9 in response to serum or insulin was only marginally affected in the SIN1-/- cells (Figure 3C). We also did not observe a difference in the kinetics of GSK3 phosphorylation between the wild-type and SIN1-/- cells (data not shown). These results suggest that the singly Thr308-phosphorylated form of Akt may be partially functional in vivo. We also examined phosphorylation of TSC2, another Akt target (Manning et al., 2002), at the Akt target sites Ser939 and Thr1462 and found no significant difference between wild-type and SIN1-/- cells upon serum and insulin stimulation (Figure 3C). Furthermore, we compared the proliferation rates of several sets of MEFs with wildtype, SIN1+/-, and SIN1-/- genotypes established from E10 embryos. No significant difference in the cell-doubling time of these MEFs was observed (Figure 3D). Finally, we did not find any size difference of wild-type and SIN1-/- cells grown under starvation or normal growth conditions (Figure 3E and data not shown). Hence, the growth factorinduced GSK3 and TSC2 phosphorylation may not fully depend on Akt-Ser473 phosphorylation. Phosphorylation at Thr24/Thr32 of FoxO1/FoxO3a, an Akt Target for the Cell-Survival Pathway, Is Defective in SIN1-/- Cells" provenance.
• _11 value "To investigate whether this partially active Akt is functional in vivo, we first examined the in vivo phosphorylation of GSK3. Surprisingly, phosphorylation of GSK3a at Ser21 and GSK3b at Ser9 in response to serum or insulin was only marginally affected in the SIN1-/- cells (Figure 3C). We also did not observe a difference in the kinetics of GSK3 phosphorylation between the wild-type and SIN1-/- cells (data not shown). These results suggest that the singly Thr308-phosphorylated form of Akt may be partially functional in vivo. We also examined phosphorylation of TSC2, another Akt target (Manning et al., 2002), at the Akt target sites Ser939 and Thr1462 and found no significant difference between wild-type and SIN1-/- cells upon serum and insulin stimulation (Figure 3C). Furthermore, we compared the proliferation rates of several sets of MEFs with wildtype, SIN1+/-, and SIN1-/- genotypes established from E10 embryos. No significant difference in the cell-doubling time of these MEFs was observed (Figure 3D). Finally, we did not find any size difference of wild-type and SIN1-/- cells grown under starvation or normal growth conditions (Figure 3E and data not shown). Hence, the growth factorinduced GSK3 and TSC2 phosphorylation may not fully depend on Akt-Ser473 phosphorylation. Phosphorylation at Thr24/Thr32 of FoxO1/FoxO3a, an Akt Target for the Cell-Survival Pathway, Is Defective in SIN1-/- Cells" provenance.
• _7 value "To investigate whether this partially active Akt is functional in vivo, we first examined the in vivo phosphorylation of GSK3. Surprisingly, phosphorylation of GSK3a at Ser21 and GSK3b at Ser9 in response to serum or insulin was only marginally affected in the SIN1-/- cells (Figure 3C). We also did not observe a difference in the kinetics of GSK3 phosphorylation between the wild-type and SIN1-/- cells (data not shown). These results suggest that the singly Thr308-phosphorylated form of Akt may be partially functional in vivo. We also examined phosphorylation of TSC2, another Akt target (Manning et al., 2002), at the Akt target sites Ser939 and Thr1462 and found no significant difference between wild-type and SIN1-/- cells upon serum and insulin stimulation (Figure 3C). Furthermore, we compared the proliferation rates of several sets of MEFs with wildtype, SIN1+/-, and SIN1-/- genotypes established from E10 embryos. No significant difference in the cell-doubling time of these MEFs was observed (Figure 3D). Finally, we did not find any size difference of wild-type and SIN1-/- cells grown under starvation or normal growth conditions (Figure 3E and data not shown). Hence, the growth factorinduced GSK3 and TSC2 phosphorylation may not fully depend on Akt-Ser473 phosphorylation. Phosphorylation at Thr24/Thr32 of FoxO1/FoxO3a, an Akt Target for the Cell-Survival Pathway, Is Defective in SIN1-/- Cells" provenance.
• _11 value "To investigate whether this partially active Akt is functional in vivo, we first examined the in vivo phosphorylation of GSK3. Surprisingly, phosphorylation of GSK3a at Ser21 and GSK3b at Ser9 in response to serum or insulin was only marginally affected in the SIN1-/- cells (Figure 3C). We also did not observe a difference in the kinetics of GSK3 phosphorylation between the wild-type and SIN1-/- cells (data not shown). These results suggest that the singly Thr308-phosphorylated form of Akt may be partially functional in vivo. We also examined phosphorylation of TSC2, another Akt target (Manning et al., 2002), at the Akt target sites Ser939 and Thr1462 and found no significant difference between wild-type and SIN1-/- cells upon serum and insulin stimulation (Figure 3C). Furthermore, we compared the proliferation rates of several sets of MEFs with wildtype, SIN1+/-, and SIN1-/- genotypes established from E10 embryos. No significant difference in the cell-doubling time of these MEFs was observed (Figure 3D). Finally, we did not find any size difference of wild-type and SIN1-/- cells grown under starvation or normal growth conditions (Figure 3E and data not shown). Hence, the growth factorinduced GSK3 and TSC2 phosphorylation may not fully depend on Akt-Ser473 phosphorylation. Phosphorylation at Thr24/Thr32 of FoxO1/FoxO3a, an Akt Target for the Cell-Survival Pathway, Is Defective in SIN1-/- Cells" provenance.
• _5 value "To investigate whether this partially active Akt is functional in vivo, we first examined the in vivo phosphorylation of GSK3. Surprisingly, phosphorylation of GSK3a at Ser21 and GSK3b at Ser9 in response to serum or insulin was only marginally affected in the SIN1-/- cells (Figure 3C). We also did not observe a difference in the kinetics of GSK3 phosphorylation between the wild-type and SIN1-/- cells (data not shown). These results suggest that the singly Thr308-phosphorylated form of Akt may be partially functional in vivo. We also examined phosphorylation of TSC2, another Akt target (Manning et al., 2002), at the Akt target sites Ser939 and Thr1462 and found no significant difference between wild-type and SIN1-/- cells upon serum and insulin stimulation (Figure 3C). Furthermore, we compared the proliferation rates of several sets of MEFs with wildtype, SIN1+/-, and SIN1-/- genotypes established from E10 embryos. No significant difference in the cell-doubling time of these MEFs was observed (Figure 3D). Finally, we did not find any size difference of wild-type and SIN1-/- cells grown under starvation or normal growth conditions (Figure 3E and data not shown). Hence, the growth factorinduced GSK3 and TSC2 phosphorylation may not fully depend on Akt-Ser473 phosphorylation. Phosphorylation at Thr24/Thr32 of FoxO1/FoxO3a, an Akt Target for the Cell-Survival Pathway, Is Defective in SIN1-/- Cells" provenance.
• _7 value "To investigate whether this partially active Akt is functional in vivo, we first examined the in vivo phosphorylation of GSK3. Surprisingly, phosphorylation of GSK3a at Ser21 and GSK3b at Ser9 in response to serum or insulin was only marginally affected in the SIN1-/- cells (Figure 3C). We also did not observe a difference in the kinetics of GSK3 phosphorylation between the wild-type and SIN1-/- cells (data not shown). These results suggest that the singly Thr308-phosphorylated form of Akt may be partially functional in vivo. We also examined phosphorylation of TSC2, another Akt target (Manning et al., 2002), at the Akt target sites Ser939 and Thr1462 and found no significant difference between wild-type and SIN1-/- cells upon serum and insulin stimulation (Figure 3C). Furthermore, we compared the proliferation rates of several sets of MEFs with wildtype, SIN1+/-, and SIN1-/- genotypes established from E10 embryos. No significant difference in the cell-doubling time of these MEFs was observed (Figure 3D). Finally, we did not find any size difference of wild-type and SIN1-/- cells grown under starvation or normal growth conditions (Figure 3E and data not shown). Hence, the growth factorinduced GSK3 and TSC2 phosphorylation may not fully depend on Akt-Ser473 phosphorylation. Phosphorylation at Thr24/Thr32 of FoxO1/FoxO3a, an Akt Target for the Cell-Survival Pathway, Is Defective in SIN1-/- Cells" provenance.
• _5 value "To investigate whether this partially active Akt is functional in vivo, we first examined the in vivo phosphorylation of GSK3. Surprisingly, phosphorylation of GSK3a at Ser21 and GSK3b at Ser9 in response to serum or insulin was only marginally affected in the SIN1-/- cells (Figure 3C). We also did not observe a difference in the kinetics of GSK3 phosphorylation between the wild-type and SIN1-/- cells (data not shown). These results suggest that the singly Thr308-phosphorylated form of Akt may be partially functional in vivo. We also examined phosphorylation of TSC2, another Akt target (Manning et al., 2002), at the Akt target sites Ser939 and Thr1462 and found no significant difference between wild-type and SIN1-/- cells upon serum and insulin stimulation (Figure 3C). Furthermore, we compared the proliferation rates of several sets of MEFs with wildtype, SIN1+/-, and SIN1-/- genotypes established from E10 embryos. No significant difference in the cell-doubling time of these MEFs was observed (Figure 3D). Finally, we did not find any size difference of wild-type and SIN1-/- cells grown under starvation or normal growth conditions (Figure 3E and data not shown). Hence, the growth factorinduced GSK3 and TSC2 phosphorylation may not fully depend on Akt-Ser473 phosphorylation. Phosphorylation at Thr24/Thr32 of FoxO1/FoxO3a, an Akt Target for the Cell-Survival Pathway, Is Defective in SIN1-/- Cells" provenance.
• _5 value "To investigate whether this partially active Akt is functional in vivo, we first examined the in vivo phosphorylation of GSK3. Surprisingly, phosphorylation of GSK3a at Ser21 and GSK3b at Ser9 in response to serum or insulin was only marginally affected in the SIN1-/- cells (Figure 3C). We also did not observe a difference in the kinetics of GSK3 phosphorylation between the wild-type and SIN1-/- cells (data not shown). These results suggest that the singly Thr308-phosphorylated form of Akt may be partially functional in vivo. We also examined phosphorylation of TSC2, another Akt target (Manning et al., 2002), at the Akt target sites Ser939 and Thr1462 and found no significant difference between wild-type and SIN1-/- cells upon serum and insulin stimulation (Figure 3C). Furthermore, we compared the proliferation rates of several sets of MEFs with wildtype, SIN1+/-, and SIN1-/- genotypes established from E10 embryos. No significant difference in the cell-doubling time of these MEFs was observed (Figure 3D). Finally, we did not find any size difference of wild-type and SIN1-/- cells grown under starvation or normal growth conditions (Figure 3E and data not shown). Hence, the growth factorinduced GSK3 and TSC2 phosphorylation may not fully depend on Akt-Ser473 phosphorylation. Phosphorylation at Thr24/Thr32 of FoxO1/FoxO3a, an Akt Target for the Cell-Survival Pathway, Is Defective in SIN1-/- Cells" provenance.