Ignet

Gene Information

Gene symbol: PIK3R2

Gene name: phosphoinositide-3-kinase, regulatory subunit 2 (beta)

HGNC ID: 8980

Synonyms: P85B, p85

Related Genes

#	Gene Symbol	Number of hits
1	AKT1	1 hits
2	CUX1	1 hits
3	PIK3CA	1 hits
4	PIK3R1	1 hits
5	PTPN11	1 hits

Related Sentences

#	PMID	Sentence
1	17881440	SH3 binding motif 1 in influenza A virus NS1 protein is essential for PI3K/Akt signaling pathway activation.
2	17881440	Recent studies have demonstrated that influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt signaling pathway by binding of influenza NS1 protein to the p85 regulatory subunit of PI3K.
3	17881440	Our previous study proposed that two polyproline motifs in NS1 (amino acids 164 to 167 [PXXP], SH3 binding motif 1, and amino acids 213 to 216 [PPXXP], SH3 binding motif 2) may mediate binding to the p85 subunit of PI3K.
4	17881440	Here we performed individual mutational analyses on these two motifs and demonstrated that SH3 binding motif 1 contributes to the interactions of NS1 with p85beta, whereas SH3 binding motif 2 is not required for this process.
5	17881440	Mutant viruses carrying NS1 with mutations in SH3 binding motif 1 failed to interact with p85beta and induce the subsequent activation of PI3K/Akt pathway.
6	17881440	Our data suggest that SH3 binding motif 1 in NS1 protein is required for NS1-p85beta interaction and PI3K/Akt activation.
7	17881440	Activation of PI3K/Akt pathway is beneficial for virus replication by inhibiting virus induced apoptosis through phosphorylation of caspase-9.
8	17881440	SH3 binding motif 1 in influenza A virus NS1 protein is essential for PI3K/Akt signaling pathway activation.
9	17881440	Recent studies have demonstrated that influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt signaling pathway by binding of influenza NS1 protein to the p85 regulatory subunit of PI3K.
10	17881440	Our previous study proposed that two polyproline motifs in NS1 (amino acids 164 to 167 [PXXP], SH3 binding motif 1, and amino acids 213 to 216 [PPXXP], SH3 binding motif 2) may mediate binding to the p85 subunit of PI3K.
11	17881440	Here we performed individual mutational analyses on these two motifs and demonstrated that SH3 binding motif 1 contributes to the interactions of NS1 with p85beta, whereas SH3 binding motif 2 is not required for this process.
12	17881440	Mutant viruses carrying NS1 with mutations in SH3 binding motif 1 failed to interact with p85beta and induce the subsequent activation of PI3K/Akt pathway.
13	17881440	Our data suggest that SH3 binding motif 1 in NS1 protein is required for NS1-p85beta interaction and PI3K/Akt activation.
14	17881440	Activation of PI3K/Akt pathway is beneficial for virus replication by inhibiting virus induced apoptosis through phosphorylation of caspase-9.
15	18534979	Mechanism of influenza A virus NS1 protein interaction with the p85beta, but not the p85alpha, subunit of phosphatidylinositol 3-kinase (PI3K) and up-regulation of PI3K activity.
16	18534979	Influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by binding influenza A virus NS1 protein to the p85beta regulatory subunit of PI3K.
17	18534979	In this study, we report that NS1 binds to the inter-SH2 (iSH2) domain of p85beta.
18	18534979	Mutational analyses on p85beta iSH2 domain defined that Val-573 is the critical amino acid (AA) that mediates NS1 and p85beta interaction.
19	18534979	In reciprocal gain of function experiments with p85alpha, we demonstrated that mutation to Val at Met-582 leads to NS1 binding and increased PI3K activity.
20	18534979	Molecular modeling based on our experimental results suggested that, in addition to the interaction interface between the NS1 SH3 binding motif 1 (AA 164-167) and p85beta Val-573, AA 137-142 in NS1 might interact with p85beta.
21	18534979	Indeed, mutations of AA 141 and 142 in NS1 disrupted the interaction between NS1 and p85beta.
22	18534979	In contrast, in the mutant virus-infected cells containing mutant NS1 unable to interact with p85beta, the p85beta-associated PI3K activity up-regulation was not seen, suggesting that PI3K up-regulation is dependent upon the interaction between NS1 and p85beta.
23	18534979	Competition experiments and the immunoprecipitation studies demonstrated that NS1, p85beta, and p110 form a complex in cells.
24	18534979	Finally, the mechanism by which binding of NS1 to p85beta regulates PI3K activity was discussed based on a predicted structural model of NS1-p85-p110 complex.
25	18534979	Mechanism of influenza A virus NS1 protein interaction with the p85beta, but not the p85alpha, subunit of phosphatidylinositol 3-kinase (PI3K) and up-regulation of PI3K activity.
26	18534979	Influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by binding influenza A virus NS1 protein to the p85beta regulatory subunit of PI3K.
27	18534979	In this study, we report that NS1 binds to the inter-SH2 (iSH2) domain of p85beta.
28	18534979	Mutational analyses on p85beta iSH2 domain defined that Val-573 is the critical amino acid (AA) that mediates NS1 and p85beta interaction.
29	18534979	In reciprocal gain of function experiments with p85alpha, we demonstrated that mutation to Val at Met-582 leads to NS1 binding and increased PI3K activity.
30	18534979	Molecular modeling based on our experimental results suggested that, in addition to the interaction interface between the NS1 SH3 binding motif 1 (AA 164-167) and p85beta Val-573, AA 137-142 in NS1 might interact with p85beta.
31	18534979	Indeed, mutations of AA 141 and 142 in NS1 disrupted the interaction between NS1 and p85beta.
32	18534979	In contrast, in the mutant virus-infected cells containing mutant NS1 unable to interact with p85beta, the p85beta-associated PI3K activity up-regulation was not seen, suggesting that PI3K up-regulation is dependent upon the interaction between NS1 and p85beta.
33	18534979	Competition experiments and the immunoprecipitation studies demonstrated that NS1, p85beta, and p110 form a complex in cells.
34	18534979	Finally, the mechanism by which binding of NS1 to p85beta regulates PI3K activity was discussed based on a predicted structural model of NS1-p85-p110 complex.
35	18534979	Mechanism of influenza A virus NS1 protein interaction with the p85beta, but not the p85alpha, subunit of phosphatidylinositol 3-kinase (PI3K) and up-regulation of PI3K activity.
36	18534979	Influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by binding influenza A virus NS1 protein to the p85beta regulatory subunit of PI3K.
37	18534979	In this study, we report that NS1 binds to the inter-SH2 (iSH2) domain of p85beta.
38	18534979	Mutational analyses on p85beta iSH2 domain defined that Val-573 is the critical amino acid (AA) that mediates NS1 and p85beta interaction.
39	18534979	In reciprocal gain of function experiments with p85alpha, we demonstrated that mutation to Val at Met-582 leads to NS1 binding and increased PI3K activity.
40	18534979	Molecular modeling based on our experimental results suggested that, in addition to the interaction interface between the NS1 SH3 binding motif 1 (AA 164-167) and p85beta Val-573, AA 137-142 in NS1 might interact with p85beta.
41	18534979	Indeed, mutations of AA 141 and 142 in NS1 disrupted the interaction between NS1 and p85beta.
42	18534979	In contrast, in the mutant virus-infected cells containing mutant NS1 unable to interact with p85beta, the p85beta-associated PI3K activity up-regulation was not seen, suggesting that PI3K up-regulation is dependent upon the interaction between NS1 and p85beta.
43	18534979	Competition experiments and the immunoprecipitation studies demonstrated that NS1, p85beta, and p110 form a complex in cells.
44	18534979	Finally, the mechanism by which binding of NS1 to p85beta regulates PI3K activity was discussed based on a predicted structural model of NS1-p85-p110 complex.
45	18534979	Mechanism of influenza A virus NS1 protein interaction with the p85beta, but not the p85alpha, subunit of phosphatidylinositol 3-kinase (PI3K) and up-regulation of PI3K activity.
46	18534979	Influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by binding influenza A virus NS1 protein to the p85beta regulatory subunit of PI3K.
47	18534979	In this study, we report that NS1 binds to the inter-SH2 (iSH2) domain of p85beta.
48	18534979	Mutational analyses on p85beta iSH2 domain defined that Val-573 is the critical amino acid (AA) that mediates NS1 and p85beta interaction.
49	18534979	In reciprocal gain of function experiments with p85alpha, we demonstrated that mutation to Val at Met-582 leads to NS1 binding and increased PI3K activity.
50	18534979	Molecular modeling based on our experimental results suggested that, in addition to the interaction interface between the NS1 SH3 binding motif 1 (AA 164-167) and p85beta Val-573, AA 137-142 in NS1 might interact with p85beta.
51	18534979	Indeed, mutations of AA 141 and 142 in NS1 disrupted the interaction between NS1 and p85beta.
52	18534979	In contrast, in the mutant virus-infected cells containing mutant NS1 unable to interact with p85beta, the p85beta-associated PI3K activity up-regulation was not seen, suggesting that PI3K up-regulation is dependent upon the interaction between NS1 and p85beta.
53	18534979	Competition experiments and the immunoprecipitation studies demonstrated that NS1, p85beta, and p110 form a complex in cells.
54	18534979	Finally, the mechanism by which binding of NS1 to p85beta regulates PI3K activity was discussed based on a predicted structural model of NS1-p85-p110 complex.
55	18534979	Mechanism of influenza A virus NS1 protein interaction with the p85beta, but not the p85alpha, subunit of phosphatidylinositol 3-kinase (PI3K) and up-regulation of PI3K activity.
56	18534979	Influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by binding influenza A virus NS1 protein to the p85beta regulatory subunit of PI3K.
57	18534979	In this study, we report that NS1 binds to the inter-SH2 (iSH2) domain of p85beta.
58	18534979	Mutational analyses on p85beta iSH2 domain defined that Val-573 is the critical amino acid (AA) that mediates NS1 and p85beta interaction.
59	18534979	In reciprocal gain of function experiments with p85alpha, we demonstrated that mutation to Val at Met-582 leads to NS1 binding and increased PI3K activity.
60	18534979	Molecular modeling based on our experimental results suggested that, in addition to the interaction interface between the NS1 SH3 binding motif 1 (AA 164-167) and p85beta Val-573, AA 137-142 in NS1 might interact with p85beta.
61	18534979	Indeed, mutations of AA 141 and 142 in NS1 disrupted the interaction between NS1 and p85beta.
62	18534979	In contrast, in the mutant virus-infected cells containing mutant NS1 unable to interact with p85beta, the p85beta-associated PI3K activity up-regulation was not seen, suggesting that PI3K up-regulation is dependent upon the interaction between NS1 and p85beta.
63	18534979	Competition experiments and the immunoprecipitation studies demonstrated that NS1, p85beta, and p110 form a complex in cells.
64	18534979	Finally, the mechanism by which binding of NS1 to p85beta regulates PI3K activity was discussed based on a predicted structural model of NS1-p85-p110 complex.
65	18534979	Mechanism of influenza A virus NS1 protein interaction with the p85beta, but not the p85alpha, subunit of phosphatidylinositol 3-kinase (PI3K) and up-regulation of PI3K activity.
66	18534979	Influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by binding influenza A virus NS1 protein to the p85beta regulatory subunit of PI3K.
67	18534979	In this study, we report that NS1 binds to the inter-SH2 (iSH2) domain of p85beta.
68	18534979	Mutational analyses on p85beta iSH2 domain defined that Val-573 is the critical amino acid (AA) that mediates NS1 and p85beta interaction.
69	18534979	In reciprocal gain of function experiments with p85alpha, we demonstrated that mutation to Val at Met-582 leads to NS1 binding and increased PI3K activity.
70	18534979	Molecular modeling based on our experimental results suggested that, in addition to the interaction interface between the NS1 SH3 binding motif 1 (AA 164-167) and p85beta Val-573, AA 137-142 in NS1 might interact with p85beta.
71	18534979	Indeed, mutations of AA 141 and 142 in NS1 disrupted the interaction between NS1 and p85beta.
72	18534979	In contrast, in the mutant virus-infected cells containing mutant NS1 unable to interact with p85beta, the p85beta-associated PI3K activity up-regulation was not seen, suggesting that PI3K up-regulation is dependent upon the interaction between NS1 and p85beta.
73	18534979	Competition experiments and the immunoprecipitation studies demonstrated that NS1, p85beta, and p110 form a complex in cells.
74	18534979	Finally, the mechanism by which binding of NS1 to p85beta regulates PI3K activity was discussed based on a predicted structural model of NS1-p85-p110 complex.
75	18534979	Mechanism of influenza A virus NS1 protein interaction with the p85beta, but not the p85alpha, subunit of phosphatidylinositol 3-kinase (PI3K) and up-regulation of PI3K activity.
76	18534979	Influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by binding influenza A virus NS1 protein to the p85beta regulatory subunit of PI3K.
77	18534979	In this study, we report that NS1 binds to the inter-SH2 (iSH2) domain of p85beta.
78	18534979	Mutational analyses on p85beta iSH2 domain defined that Val-573 is the critical amino acid (AA) that mediates NS1 and p85beta interaction.
79	18534979	In reciprocal gain of function experiments with p85alpha, we demonstrated that mutation to Val at Met-582 leads to NS1 binding and increased PI3K activity.
80	18534979	Molecular modeling based on our experimental results suggested that, in addition to the interaction interface between the NS1 SH3 binding motif 1 (AA 164-167) and p85beta Val-573, AA 137-142 in NS1 might interact with p85beta.
81	18534979	Indeed, mutations of AA 141 and 142 in NS1 disrupted the interaction between NS1 and p85beta.
82	18534979	In contrast, in the mutant virus-infected cells containing mutant NS1 unable to interact with p85beta, the p85beta-associated PI3K activity up-regulation was not seen, suggesting that PI3K up-regulation is dependent upon the interaction between NS1 and p85beta.
83	18534979	Competition experiments and the immunoprecipitation studies demonstrated that NS1, p85beta, and p110 form a complex in cells.
84	18534979	Finally, the mechanism by which binding of NS1 to p85beta regulates PI3K activity was discussed based on a predicted structural model of NS1-p85-p110 complex.
85	18534979	Mechanism of influenza A virus NS1 protein interaction with the p85beta, but not the p85alpha, subunit of phosphatidylinositol 3-kinase (PI3K) and up-regulation of PI3K activity.
86	18534979	Influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by binding influenza A virus NS1 protein to the p85beta regulatory subunit of PI3K.
87	18534979	In this study, we report that NS1 binds to the inter-SH2 (iSH2) domain of p85beta.
88	18534979	Mutational analyses on p85beta iSH2 domain defined that Val-573 is the critical amino acid (AA) that mediates NS1 and p85beta interaction.
89	18534979	In reciprocal gain of function experiments with p85alpha, we demonstrated that mutation to Val at Met-582 leads to NS1 binding and increased PI3K activity.
90	18534979	Molecular modeling based on our experimental results suggested that, in addition to the interaction interface between the NS1 SH3 binding motif 1 (AA 164-167) and p85beta Val-573, AA 137-142 in NS1 might interact with p85beta.
91	18534979	Indeed, mutations of AA 141 and 142 in NS1 disrupted the interaction between NS1 and p85beta.
92	18534979	In contrast, in the mutant virus-infected cells containing mutant NS1 unable to interact with p85beta, the p85beta-associated PI3K activity up-regulation was not seen, suggesting that PI3K up-regulation is dependent upon the interaction between NS1 and p85beta.
93	18534979	Competition experiments and the immunoprecipitation studies demonstrated that NS1, p85beta, and p110 form a complex in cells.
94	18534979	Finally, the mechanism by which binding of NS1 to p85beta regulates PI3K activity was discussed based on a predicted structural model of NS1-p85-p110 complex.
95	18534979	Mechanism of influenza A virus NS1 protein interaction with the p85beta, but not the p85alpha, subunit of phosphatidylinositol 3-kinase (PI3K) and up-regulation of PI3K activity.
96	18534979	Influenza A virus infection activates the phosphatidylinositol 3-kinase (PI3K)/Akt pathway by binding influenza A virus NS1 protein to the p85beta regulatory subunit of PI3K.
97	18534979	In this study, we report that NS1 binds to the inter-SH2 (iSH2) domain of p85beta.
98	18534979	Mutational analyses on p85beta iSH2 domain defined that Val-573 is the critical amino acid (AA) that mediates NS1 and p85beta interaction.
99	18534979	In reciprocal gain of function experiments with p85alpha, we demonstrated that mutation to Val at Met-582 leads to NS1 binding and increased PI3K activity.
100	18534979	Molecular modeling based on our experimental results suggested that, in addition to the interaction interface between the NS1 SH3 binding motif 1 (AA 164-167) and p85beta Val-573, AA 137-142 in NS1 might interact with p85beta.
101	18534979	Indeed, mutations of AA 141 and 142 in NS1 disrupted the interaction between NS1 and p85beta.
102	18534979	In contrast, in the mutant virus-infected cells containing mutant NS1 unable to interact with p85beta, the p85beta-associated PI3K activity up-regulation was not seen, suggesting that PI3K up-regulation is dependent upon the interaction between NS1 and p85beta.
103	18534979	Competition experiments and the immunoprecipitation studies demonstrated that NS1, p85beta, and p110 form a complex in cells.
104	18534979	Finally, the mechanism by which binding of NS1 to p85beta regulates PI3K activity was discussed based on a predicted structural model of NS1-p85-p110 complex.