| Type |
Details |
Score |
| Publication |
| First Author: |
Salt I |
| Year: |
1998 |
| Journal: |
Biochem J |
| Title: |
AMP-activated protein kinase: greater AMP dependence, and preferential nuclear localization, of complexes containing the alpha2 isoform. |
| Volume: |
334 ( Pt 1) |
|
| Pages: |
177-87 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
AMPK, a serine/threonine protein kinase (STK), catalyzes the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. It acts as a sensor for the energy status of the cell and is activated by cellular stresses that lead to ATP depletion such as hypoxia, heat shock, and glucose deprivation, among others. AMPK is a heterotrimer of three subunits: alpha, beta, and gamma []. The alpha subunit is the catalytic subunit and it contains an N-terminal kinase domain, a putative autoinhibitory domain (AID) and a C-terminal region required for beta subunit binding. The beta scaffolding subunit mediates AMPK assembly by bridging alpha and gamma subunits. The C-terminal domain of the AMPK alpha 1 subunit interacts with the C-terminal region of the beta subunit to form a tight alpha-beta complex that is associated with the gamma subunit. The AMPK alpha subunit auto-inhibitory region interacts with the kinase domain; this inhibition is negated by the interaction with the AMPK gamma subunit [].AMPK has been implicated in a number of diseases related to energy metabolism including type 2 diabetes, obesity and cancer [, ]. AMPK is activated by rising AMP concentrations coupled with falling ATP concentrations. Activation of AMPK is also dependent on the phosphorylation of alpha subunit by upstream kinases such as LKB1 [].Vertebrates contain two isoforms of the alpha subunit, alpha1 and alpha2, which are encoded by different genes, PRKAA1 and PRKAA2, respectively, and show varying expression patterns. AMPKalpha2 shows cytoplasmic and nuclear localization, whereas AMPKalpha1 is localized only in the cytoplasm [, ]. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Jeyabalan J |
| Year: |
2012 |
| Journal: |
J Endocrinol |
| Title: |
Mice lacking AMP-activated protein kinase α1 catalytic subunit have increased bone remodelling and modified skeletal responses to hormonal challenges induced by ovariectomy and intermittent PTH treatment. |
| Volume: |
214 |
| Issue: |
3 |
| Pages: |
349-58 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
AMPK, a serine/threonine protein kinase (STK), catalyzes the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. It acts as a sensor for the energy status of the cell and is activated by cellular stresses that lead to ATP depletion such as hypoxia, heat shock, and glucose deprivation, among others. AMPK is a heterotrimer of three subunits: alpha, beta, and gamma []. The alpha subunit is the catalytic subunit and it contains an N-terminal kinase domain, a putative autoinhibitory domain (AID) and a C-terminal region required for beta subunit binding. The beta scaffolding subunit mediates AMPK assembly by bridging alpha and gamma subunits. The C-terminal domain of the AMPK alpha 1 subunit interacts with the C-terminal region of the beta subunit to form a tightalpha-beta complex that is associated with the gamma subunit. The AMPK alpha subunit auto-inhibitory region interacts with the kinase domain; this inhibition is negated by the interaction with the AMPK gamma subunit [].AMPK has been implicated in a number of diseases related to energy metabolism including type 2 diabetes, obesity and cancer [, ]. AMPK is activated by rising AMP concentrations coupled with falling ATP concentrations. Activation of AMPK is also dependent on the phosphorylation of alpha subunit by upstream kinases such as LKB1 [].Vertebrates contain two isoforms of the alpha subunit, alpha1 and alpha2, which are encoded by different genes, PRKAA1 and PRKAA2, respectively, and show varying expression patterns. AMPKalpha1 is the predominant isoform expressed in bone; it plays a role in bone remodeling in response to hormonal regulation []. AMPK alpha1 impacts the regulation of fat metabolism []. It also mediates the vasoprotective effects of estrogen through phosphorylation of another in vivo substrate, RhoA []. |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
180
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
550
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sanz P |
| Year: |
2008 |
| Journal: |
Curr Protein Pept Sci |
| Title: |
AMP-activated protein kinase: structure and regulation. |
| Volume: |
9 |
| Issue: |
5 |
| Pages: |
478-92 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Cool B |
| Year: |
2006 |
| Journal: |
Cell Metab |
| Title: |
Identification and characterization of a small molecule AMPK activator that treats key components of type 2 diabetes and the metabolic syndrome. |
| Volume: |
3 |
| Issue: |
6 |
| Pages: |
403-16 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Shackelford DB |
| Year: |
2009 |
| Journal: |
Nat Rev Cancer |
| Title: |
The LKB1-AMPK pathway: metabolism and growth control in tumour suppression. |
| Volume: |
9 |
| Issue: |
8 |
| Pages: |
563-75 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Woods A |
| Year: |
2003 |
| Journal: |
Curr Biol |
| Title: |
LKB1 is the upstream kinase in the AMP-activated protein kinase cascade. |
| Volume: |
13 |
| Issue: |
22 |
| Pages: |
2004-8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zhu L |
| Year: |
2011 |
| Journal: |
Structure |
| Title: |
Structural insights into the architecture and allostery of full-length AMP-activated protein kinase. |
| Volume: |
19 |
| Issue: |
4 |
| Pages: |
515-22 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
552
|
| Fragment?: |
false |
|
•
•
•
•
•
|
