Supplier: Bioss

AMPK is a heterotrimeric complex comprising a catalytic a subunit and regulatory b and g subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxy-methylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKa1 and AMPKa2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKb1 encodes a 271 amino acid protein and human AMPKb2 encodes a 272 amino acid protein. The human AMPKg1 gene encodes a 331 amino acid protein. Human AMPKg2 and AMPKg3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.

Supplier: Bioss

AMPK is a heterotrimeric complex comprising a catalytic a subunit and regulatory b and g subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxy-methylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKa1 and AMPKa2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKb1 encodes a 271 amino acid protein and human AMPKb2 encodes a 272 amino acid protein. The human AMPKg1 gene encodes a 331 amino acid protein. Human AMPKg2 and AMPKg3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.

Supplier: Bioss

AMPK is a heterotrimeric complex comprising a catalytic a subunit and regulatory b and g subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxy-methylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKa1 and AMPKa2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKb1 encodes a 271 amino acid protein and human AMPKb2 encodes a 272 amino acid protein. The human AMPKg1 gene encodes a 331 amino acid protein. Human AMPKg2 and AMPKg3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.

Supplier: Bioss

AMPK is a heterotrimeric complex comprising a catalytic a subunit and regulatory b and g subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxy-methylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKa1 and AMPKa2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKb1 encodes a 271 amino acid protein and human AMPKb2 encodes a 272 amino acid protein. The human AMPKg1 gene encodes a 331 amino acid protein. Human AMPKg2 and AMPKg3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.

Supplier: Bioss

AMPK is a heterotrimeric complex comprising a catalytic a subunit and regulatory b and g subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxy-methylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKa1 and AMPKa2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKb1 encodes a 271 amino acid protein and human AMPKb2 encodes a 272 amino acid protein. The human AMPKg1 gene encodes a 331 amino acid protein. Human AMPKg2 and AMPKg3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.

Supplier: Aviva Systems Biology

activating transcription factor 6 Cyclic AMP-dependent transcription factor ATF-6 alpha 1 * 50 µl

Supplier: Bioss

AMPK is a heterotrimeric complex comprising a catalytic a subunit and regulatory b and g subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxy-methylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKa1 and AMPKa2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKb1 encodes a 271 amino acid protein and human AMPKb2 encodes a 272 amino acid protein. The human AMPKg1 gene encodes a 331 amino acid protein. Human AMPKg2 and AMPKg3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.

Supplier: Bioss

AMPK is a heterotrimeric complex comprising a catalytic a subunit and regulatory b and g subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxy-methylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKa1 and AMPKa2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKb1 encodes a 271 amino acid protein and human AMPKb2 encodes a 272 amino acid protein. The human AMPKg1 gene encodes a 331 amino acid protein. Human AMPKg2 and AMPKg3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.

Supplier: Bioss

AMPK is a heterotrimeric complex comprising a catalytic a subunit and regulatory b and g subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxy-methylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKa1 and AMPKa2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKb1 encodes a 271 amino acid protein and human AMPKb2 encodes a 272 amino acid protein. The human AMPKg1 gene encodes a 331 amino acid protein. Human AMPKg2 and AMPKg3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.

Supplier: Bioss

AMPK is a heterotrimeric complex comprising a catalytic a subunit and regulatory b and g subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxy-methylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKa1 and AMPKa2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKb1 encodes a 271 amino acid protein and human AMPKb2 encodes a 272 amino acid protein. The human AMPKg1 gene encodes a 331 amino acid protein. Human AMPKg2 and AMPKg3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.

Supplier: Bioss

AMPK is a heterotrimeric complex comprising a catalytic a subunit and regulatory b and g subunits. It protects cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is activated by high AMP and low ATP through a mechanism involving allosteric regulation, promotion of phosphorylation by an upstream protein kinase known as AMPK kinase and inhibition of dephosphorylation. Activated AMPK can phosphorylate and regulate in vivo hydroxy-methylglutaryl-CoA reductase and acetyl-CoA carboxylase, which are key regulatory enzymes of sterol synthesis and fatty acid synthesis, respectively. The human AMPKa1 and AMPKa2 genes encode 548 amino acid and 552 amino acid proteins, respectively. Human AMPKb1 encodes a 271 amino acid protein and human AMPKb2 encodes a 272 amino acid protein. The human AMPKg1 gene encodes a 331 amino acid protein. Human AMPKg2 and AMPKg3, which are 569 and 492 amino acid proteins, respectively, contain unique N-terminal domains and may participate directly in the binding of AMP within the AMPK complex.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioss

PRKAB2 ans PRKAB1 are regulatory subunits of the AMP-activated protein kinase (AMPK). AMPK is a heterotrimer consisting of an alpha catalytic subunit, and non-catalytic beta and gamma subunits. AMPK is an important energy-sensing enzyme that monitors cellular energy status and plays a role in protecting cells from stresses that cause ATP depletion by switching off ATP-consuming biosynthetic pathways. AMPK is responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase (ACC). It also regulates cholesterol synthesis via phosphorylation and inactivation of hydroxymethylglutaryl-CoA reductase (HMGCR) and hormone-sensitive lipase. PRKAB2 may be a positive regulator of AMPK activity.

Supplier: Bioworld Technology

The 5-AMP activated protein kinase (AMPK), a member of the SNF1 (sucrose non fermentor) kinase family, is a heterotrimeric protein c omprise of alpha (63 kDa), beta (30 kDa) and gamma (38 kDa) subunits. 1 * 100 µG

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Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.

Supplier: Bioss

Mouse protein 25 alpha (MO25 alpha, CAB39) is a 40-kDa protein that, together with the STE20-related adaptor-alpha (STRAD alpha) pseudo kinase, forms a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase. The latter is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). CAB39 binds directly to a conserved Trp-Glu-Phe sequence at the STRAD alpha C terminus, markedly enhancing binding of STRAD alpha to LKB1 and increasing LKB1 catalytic activity. Skeletal muscle contraction results in the phosphorylation and activation of the AMP-activated protein kinase (AMPK) by an upstream kinase (AMPKK). The LKB1-STE-related adaptor (STRAD)-mouse protein 25 (MO25) complex is the major AMPKK in skeletal muscle; however, LKB1-STRAD-MO25 activity is not increased by muscle contraction. This relationship suggests that phosphorylation of AMPK by LKB1-STRAD-MO25 during skeletal muscle contraction may be regulated by allosteric mechanisms.