Ignet

Gene Information

Gene symbol: EIF2B1

Gene name: eukaryotic translation initiation factor 2B, subunit 1 alpha, 26kDa

HGNC ID: 3257

Synonyms: EIF-2Balpha, EIF-2B, EIF2BA

Related Genes

#	Gene Symbol	Number of hits
1	CSNK2A1	1 hits
2	EEF1D	1 hits
3	EIF2S1	1 hits
4	IGF1	1 hits
5	INS	1 hits
6	PDIK1L	1 hits

Related Sentences

#	PMID	Sentence
1	1777648	In other systems eIF-2B activity is regulated by phosphorylation of the alpha-subunit of a second initiation factor, eIF-2.
2	7893823	In liver treated with calcium-mobilizing hormones, the reduction in eIF-2B activity is the result of an increase in the phosphorylation state of the alpha-subunit of a second initiation factor, eIF-2.
3	7893823	In contrast, the inhibition of initiation that occurs in skeletal muscle deprived of insulin is not due to a change in the phosphorylation state of eIF-2 alpha.
4	8430778	The activity of casein kinase II, which can phosphorylate and activate eIF-2B in vitro, was significantly lower in extracts of fast-twitch, but not cardiac muscle, of diabetic rats compared with controls.
5	8430778	The results presented here demonstrate that changes in eIF-2 alpha phosphorylation are not responsible for the effect of diabetes on eIF-2B activity in fast-twitch skeletal muscle.
6	8430778	The activity of casein kinase II, which can phosphorylate and activate eIF-2B in vitro, was significantly lower in extracts of fast-twitch, but not cardiac muscle, of diabetic rats compared with controls.
7	8430778	The results presented here demonstrate that changes in eIF-2 alpha phosphorylation are not responsible for the effect of diabetes on eIF-2B activity in fast-twitch skeletal muscle.
8	8777248	To study the effect of prolonged diabetes on protein synthesis and on the activities of initiation factors eIF-2 and eIF-2B in the liver, female rats were treated with streptozotocin.
9	8777248	The isoelectric forms of the beta subunit of eIF-2 factor, eIF-2 beta, were different in the diabetic and the control animals, indicating that insulin deficiency modifies the phosphorylation of specific substrates.
10	8777248	Since no differences were detected in RNA or eIF-2 content between control and diabetic rats, translation may, at least partly, be inhibited in the liver by an impairment of peptide chain initiation caused by the decreased eIF-2B activity which nevertheless is independent of eIF-2 alpha phosphorylation.
11	8777248	To study the effect of prolonged diabetes on protein synthesis and on the activities of initiation factors eIF-2 and eIF-2B in the liver, female rats were treated with streptozotocin.
12	8777248	The isoelectric forms of the beta subunit of eIF-2 factor, eIF-2 beta, were different in the diabetic and the control animals, indicating that insulin deficiency modifies the phosphorylation of specific substrates.
13	8777248	Since no differences were detected in RNA or eIF-2 content between control and diabetic rats, translation may, at least partly, be inhibited in the liver by an impairment of peptide chain initiation caused by the decreased eIF-2B activity which nevertheless is independent of eIF-2 alpha phosphorylation.
14	10198309	These studies determined whether insulin-like growth factor-I (IGF-I) involvement in exercise-stimulated anabolic processes becomes more evident during hypoinsulinemia.
15	10198309	This preserved response may be due to a compensatory increase in muscle IGF-I content and a maintained ability to activate eIF2B.
16	10216953	Eukaryotic initiation factor eIF2B is a guanine nucleotide exchange protein involved in regulation of translation initiation.
17	10216953	Phosphorylation of the epsilon-subunit is thought to be important in insulin-mediated changes in eIF2B activity.
18	10216953	However, elucidation of insulin's action has proven elusive, primarily because eIF2B epsilon is a substrate in vitro for at least three different protein kinases.
19	10216953	Treating diabetic rats with insulin rapidly reduced eIF2B epsilon kinase activity below control values.
20	10216953	Based on the pattern of phosphorylation of the wildtype and two variant forms of eIF2B epsilon using casein kinase (CK)-I, CK-II, or GSK-3 as well as that observed with skeletal muscle extracts, we conclude that the predominant eIF2B epsilon kinase in psoas muscle is GSK-3.
21	10216953	Thus, insulin-mediated changes in eIF2B activity are likely to involve GSK-3.
22	10216953	Eukaryotic initiation factor eIF2B is a guanine nucleotide exchange protein involved in regulation of translation initiation.
23	10216953	Phosphorylation of the epsilon-subunit is thought to be important in insulin-mediated changes in eIF2B activity.
24	10216953	However, elucidation of insulin's action has proven elusive, primarily because eIF2B epsilon is a substrate in vitro for at least three different protein kinases.
25	10216953	Treating diabetic rats with insulin rapidly reduced eIF2B epsilon kinase activity below control values.
26	10216953	Based on the pattern of phosphorylation of the wildtype and two variant forms of eIF2B epsilon using casein kinase (CK)-I, CK-II, or GSK-3 as well as that observed with skeletal muscle extracts, we conclude that the predominant eIF2B epsilon kinase in psoas muscle is GSK-3.
27	10216953	Thus, insulin-mediated changes in eIF2B activity are likely to involve GSK-3.
28	10216953	Eukaryotic initiation factor eIF2B is a guanine nucleotide exchange protein involved in regulation of translation initiation.
29	10216953	Phosphorylation of the epsilon-subunit is thought to be important in insulin-mediated changes in eIF2B activity.
30	10216953	However, elucidation of insulin's action has proven elusive, primarily because eIF2B epsilon is a substrate in vitro for at least three different protein kinases.
31	10216953	Treating diabetic rats with insulin rapidly reduced eIF2B epsilon kinase activity below control values.
32	10216953	Based on the pattern of phosphorylation of the wildtype and two variant forms of eIF2B epsilon using casein kinase (CK)-I, CK-II, or GSK-3 as well as that observed with skeletal muscle extracts, we conclude that the predominant eIF2B epsilon kinase in psoas muscle is GSK-3.
33	10216953	Thus, insulin-mediated changes in eIF2B activity are likely to involve GSK-3.
34	10216953	Eukaryotic initiation factor eIF2B is a guanine nucleotide exchange protein involved in regulation of translation initiation.
35	10216953	Phosphorylation of the epsilon-subunit is thought to be important in insulin-mediated changes in eIF2B activity.
36	10216953	However, elucidation of insulin's action has proven elusive, primarily because eIF2B epsilon is a substrate in vitro for at least three different protein kinases.
37	10216953	Treating diabetic rats with insulin rapidly reduced eIF2B epsilon kinase activity below control values.
38	10216953	Based on the pattern of phosphorylation of the wildtype and two variant forms of eIF2B epsilon using casein kinase (CK)-I, CK-II, or GSK-3 as well as that observed with skeletal muscle extracts, we conclude that the predominant eIF2B epsilon kinase in psoas muscle is GSK-3.
39	10216953	Thus, insulin-mediated changes in eIF2B activity are likely to involve GSK-3.
40	10216953	Eukaryotic initiation factor eIF2B is a guanine nucleotide exchange protein involved in regulation of translation initiation.
41	10216953	Phosphorylation of the epsilon-subunit is thought to be important in insulin-mediated changes in eIF2B activity.
42	10216953	However, elucidation of insulin's action has proven elusive, primarily because eIF2B epsilon is a substrate in vitro for at least three different protein kinases.
43	10216953	Treating diabetic rats with insulin rapidly reduced eIF2B epsilon kinase activity below control values.
44	10216953	Based on the pattern of phosphorylation of the wildtype and two variant forms of eIF2B epsilon using casein kinase (CK)-I, CK-II, or GSK-3 as well as that observed with skeletal muscle extracts, we conclude that the predominant eIF2B epsilon kinase in psoas muscle is GSK-3.
45	10216953	Thus, insulin-mediated changes in eIF2B activity are likely to involve GSK-3.
46	10216953	Eukaryotic initiation factor eIF2B is a guanine nucleotide exchange protein involved in regulation of translation initiation.
47	10216953	Phosphorylation of the epsilon-subunit is thought to be important in insulin-mediated changes in eIF2B activity.
48	10216953	However, elucidation of insulin's action has proven elusive, primarily because eIF2B epsilon is a substrate in vitro for at least three different protein kinases.
49	10216953	Treating diabetic rats with insulin rapidly reduced eIF2B epsilon kinase activity below control values.
50	10216953	Based on the pattern of phosphorylation of the wildtype and two variant forms of eIF2B epsilon using casein kinase (CK)-I, CK-II, or GSK-3 as well as that observed with skeletal muscle extracts, we conclude that the predominant eIF2B epsilon kinase in psoas muscle is GSK-3.
51	10216953	Thus, insulin-mediated changes in eIF2B activity are likely to involve GSK-3.
52	11408416	A potential mechanism through which insulin can stimulate protein synthesis is modulation of the activity of eukaryotic initiation factor 2B (eIF2B).
53	12837665	The purpose of the study described herein was to investigate how the mammalian target of rapamycin (mTOR)-signaling pathway and eukaryotic initiation factor 2B (eIF2B) activity, both having key roles in the translational control of protein synthesis in skeletal muscle, are regulated in cardiac muscle of rats in response to two different models of altered free fatty acid (FFA) and insulin availability.