Ignet

Gene Information

Gene symbol: MLXIP

Gene name: MLX interacting protein

HGNC ID: 17055

Synonyms: MONDOA, KIAA0867, MIR, bHLHe36

Related Genes

#	Gene Symbol	Number of hits
1	ADIPOR1	1 hits
2	MIRN192	1 hits
3	MLX	1 hits
4	MLXIPL	1 hits
5	NFE2L2	1 hits
6	NR1H3	1 hits
7	NR3C2	1 hits
8	SLC9A3R2	1 hits
9	SREBF1	1 hits
10	TGFB1	1 hits
11	TXN	1 hits
12	TXNIP	1 hits
13	VDR	1 hits
14	ZEB2	1 hits

Related Sentences

#	PMID	Sentence
1	17360662	MicroRNA-192 in diabetic kidney glomeruli and its function in TGF-beta-induced collagen expression via inhibition of E-box repressors.
2	17360662	Key features of diabetic nephropathy (DN) include the accumulation of extracellular matrix proteins such as collagen 1-alpha 1 and -2 (Col1a1 and -2).
3	17360662	Transforming growth factor beta1 (TGF-beta), a key regulator of these extracellular matrix genes, is increased in mesangial cells (MC) in DN.
4	17360662	By microarray profiling, we noted that TGF-beta increased Col1a2 mRNA in mouse MC (MMC) but also decreased mRNA levels of an E-box repressor, deltaEF1.
5	17360662	TGF-beta treatment or short hairpin RNAs targeting deltaEF1 increased enhancer activity of upstream E-box elements in the Col1a2 gene.
6	17360662	TGF-beta also decreased the expression of Smad-interacting protein 1 (SIP1), another E-box repressor similar to deltaEF1.
7	17360662	Interestingly, we noted that SIP1 is a target of microRNA-192 (miR-192), a key miR highly expressed in the kidney. miR-192 levels also were increased by TGF-beta in MMC.
8	17360662	TGF-beta treatment or transfection with miR-192 decreased endogenous SIP1 expression as well as reporter activity of a SIP1 3' UTR-containing luciferase construct in MMC.
9	17360662	Conversely, a miR-192 inhibitor enhanced the luciferase activity, confirming SIP1 to be a miR-192 target.
10	17360662	Furthermore, miR-192 synergized with deltaEF1 short hairpin RNAs to increase Col1a2 E-box-luc activity.
11	17360662	Importantly, the in vivo relevance was noted by the observation that miR-192 levels were enhanced significantly in glomeruli isolated from streptozotocin-injected diabetic mice as well as diabetic db/db mice relative to corresponding nondiabetic controls, in parallel with increased TGF-beta and Col1a2 levels.
12	17360662	These results uncover a role for miRs in the kidney and DN in controlling TGF-beta-induced Col1a2 expression by down-regulating E-box repressors.
13	21622171	We present an argument for the existence of an "extended" Myc network comprised of two related transcription factors MondoA and ChREBP.
14	21622171	Both MondoA and ChREBP sense glycolytic flux and are the principal regulators of glucose-dependent transcription in their respective tissues, skeletal muscle and liver.
15	21622171	MondoA also senses glutaminolytic flux into the tricarboxylic acid cycle and appears to coordinate the utilization of glucose and glutamine by regulating expression of thioredoxin interacting protein.
16	21622171	We present an argument for the existence of an "extended" Myc network comprised of two related transcription factors MondoA and ChREBP.
17	21622171	Both MondoA and ChREBP sense glycolytic flux and are the principal regulators of glucose-dependent transcription in their respective tissues, skeletal muscle and liver.
18	21622171	MondoA also senses glutaminolytic flux into the tricarboxylic acid cycle and appears to coordinate the utilization of glucose and glutamine by regulating expression of thioredoxin interacting protein.
19	21622171	We present an argument for the existence of an "extended" Myc network comprised of two related transcription factors MondoA and ChREBP.
20	21622171	Both MondoA and ChREBP sense glycolytic flux and are the principal regulators of glucose-dependent transcription in their respective tissues, skeletal muscle and liver.
21	21622171	MondoA also senses glutaminolytic flux into the tricarboxylic acid cycle and appears to coordinate the utilization of glucose and glutamine by regulating expression of thioredoxin interacting protein.
22	22506051	In vertebrates, the transcription factor ChREBP is a major component in glucose metabolism, while its ortholog MondoA is involved in glucose uptake.
23	22506051	Both MondoA and ChREBP contain five Mondo conserved regions (MCRI-V) that affect their cellular localization and transactivation ability.
24	22506051	While phosphorylation has been shown to affect ChREBP function, the mechanisms controlling glucose response of both ChREBP and MondoA remain elusive.
25	22506051	By incorporating sequence analysis techniques, structure predictions, and functional annotations, we synthesized data surrounding Mondo family proteins into a cohesive, accurate, and general model involving the MCRs and two additional domains that determine ChREBP and MondoA glucose response.
26	22506051	These interactions are likely involved in altering ChREBP and MondoA conformation to form an active complex and induce transcription of genes involved in glucose metabolism and lipogenesis.
27	22506051	In vertebrates, the transcription factor ChREBP is a major component in glucose metabolism, while its ortholog MondoA is involved in glucose uptake.
28	22506051	Both MondoA and ChREBP contain five Mondo conserved regions (MCRI-V) that affect their cellular localization and transactivation ability.
29	22506051	While phosphorylation has been shown to affect ChREBP function, the mechanisms controlling glucose response of both ChREBP and MondoA remain elusive.
30	22506051	By incorporating sequence analysis techniques, structure predictions, and functional annotations, we synthesized data surrounding Mondo family proteins into a cohesive, accurate, and general model involving the MCRs and two additional domains that determine ChREBP and MondoA glucose response.
31	22506051	These interactions are likely involved in altering ChREBP and MondoA conformation to form an active complex and induce transcription of genes involved in glucose metabolism and lipogenesis.
32	22506051	In vertebrates, the transcription factor ChREBP is a major component in glucose metabolism, while its ortholog MondoA is involved in glucose uptake.
33	22506051	Both MondoA and ChREBP contain five Mondo conserved regions (MCRI-V) that affect their cellular localization and transactivation ability.
34	22506051	While phosphorylation has been shown to affect ChREBP function, the mechanisms controlling glucose response of both ChREBP and MondoA remain elusive.
35	22506051	By incorporating sequence analysis techniques, structure predictions, and functional annotations, we synthesized data surrounding Mondo family proteins into a cohesive, accurate, and general model involving the MCRs and two additional domains that determine ChREBP and MondoA glucose response.
36	22506051	These interactions are likely involved in altering ChREBP and MondoA conformation to form an active complex and induce transcription of genes involved in glucose metabolism and lipogenesis.
37	22506051	In vertebrates, the transcription factor ChREBP is a major component in glucose metabolism, while its ortholog MondoA is involved in glucose uptake.
38	22506051	Both MondoA and ChREBP contain five Mondo conserved regions (MCRI-V) that affect their cellular localization and transactivation ability.
39	22506051	While phosphorylation has been shown to affect ChREBP function, the mechanisms controlling glucose response of both ChREBP and MondoA remain elusive.
40	22506051	By incorporating sequence analysis techniques, structure predictions, and functional annotations, we synthesized data surrounding Mondo family proteins into a cohesive, accurate, and general model involving the MCRs and two additional domains that determine ChREBP and MondoA glucose response.
41	22506051	These interactions are likely involved in altering ChREBP and MondoA conformation to form an active complex and induce transcription of genes involved in glucose metabolism and lipogenesis.
42	22506051	In vertebrates, the transcription factor ChREBP is a major component in glucose metabolism, while its ortholog MondoA is involved in glucose uptake.
43	22506051	Both MondoA and ChREBP contain five Mondo conserved regions (MCRI-V) that affect their cellular localization and transactivation ability.
44	22506051	While phosphorylation has been shown to affect ChREBP function, the mechanisms controlling glucose response of both ChREBP and MondoA remain elusive.
45	22506051	By incorporating sequence analysis techniques, structure predictions, and functional annotations, we synthesized data surrounding Mondo family proteins into a cohesive, accurate, and general model involving the MCRs and two additional domains that determine ChREBP and MondoA glucose response.
46	22506051	These interactions are likely involved in altering ChREBP and MondoA conformation to form an active complex and induce transcription of genes involved in glucose metabolism and lipogenesis.
47	23840567	From the 21 studied single nucleotide polymorphisms (SNPs) of seven candidate genes: MLXIPL, MLXIP, MLX, ADIPOR1, VDR, SREBF1 and NR1H3, only one tag SNP rs4758685 (T→C) was found to be statistically associated with CHD (P-value = 0.02, Odds ratio (OR) of 0.83).
48	22869588	Redox regulation by nuclear factor erythroid 2-related factor 2: gatekeeping for the basal and diabetes-induced expression of thioredoxin-interacting protein.
49	22869588	Nuclear factor erythroid 2-related factor 2 (Nrf2) is a transcription factor activated by a range of oxidants and electrophiles.
50	22869588	A pathway-focused gene array revealed that Nrf2 controls the expression of 24 genes in the heart, including the gene encoding thioredoxin-interacting protein (TXNIP).
51	22869588	Nrf2 suppressed the basal expression of Txnip in the heart and blocked induction of Txnip by high glucose by binding to an antioxidant response element (ARE) (-1286 to -1276) of the Txnip promoter.
52	22869588	Binding of Nrf2 to ARE also suppressed the binding of MondoA to the carbohydrate response element with or without high glucose.
53	22869588	On the other hand, Nrf2 boosted thioredoxin activity by inhibiting Txnip.
54	22869588	The findings revealed, for the first time, that Nrf2 is a key gatekeeper of Txnip transcription, suppressing both its basal expression and MondoA-driven induction to control the thioredoxin redox signaling in diabetes.
55	22869588	Redox regulation by nuclear factor erythroid 2-related factor 2: gatekeeping for the basal and diabetes-induced expression of thioredoxin-interacting protein.
56	22869588	Nuclear factor erythroid 2-related factor 2 (Nrf2) is a transcription factor activated by a range of oxidants and electrophiles.
57	22869588	A pathway-focused gene array revealed that Nrf2 controls the expression of 24 genes in the heart, including the gene encoding thioredoxin-interacting protein (TXNIP).
58	22869588	Nrf2 suppressed the basal expression of Txnip in the heart and blocked induction of Txnip by high glucose by binding to an antioxidant response element (ARE) (-1286 to -1276) of the Txnip promoter.
59	22869588	Binding of Nrf2 to ARE also suppressed the binding of MondoA to the carbohydrate response element with or without high glucose.
60	22869588	On the other hand, Nrf2 boosted thioredoxin activity by inhibiting Txnip.
61	22869588	The findings revealed, for the first time, that Nrf2 is a key gatekeeper of Txnip transcription, suppressing both its basal expression and MondoA-driven induction to control the thioredoxin redox signaling in diabetes.