| dc.creator |
Viana, Rosa |
|
| dc.creator |
Towler, Mhairi |
|
| dc.creator |
Pan, David A. |
|
| dc.creator |
Carling, David |
|
| dc.creator |
Viollet, Benoit |
|
| dc.creator |
Hardie, D. Grahame |
|
| dc.creator |
Sanz, Pascual |
|
| dc.date |
2008-04-15T10:27:53Z |
|
| dc.date |
2008-04-15T10:27:53Z |
|
| dc.date |
2007-04-02 |
|
| dc.date.accessioned |
2017-01-31T01:02:19Z |
|
| dc.date.available |
2017-01-31T01:02:19Z |
|
| dc.identifier |
J Biol Chem. 2007 June 1; 282(22): 16117–16125. |
|
| dc.identifier |
0021-9258 |
|
| dc.identifier |
http://hdl.handle.net/10261/3584 |
|
| dc.identifier |
10.1074/jbc.M611804200 |
|
| dc.identifier.uri |
http://dspace.mediu.edu.my:8181/xmlui/handle/10261/3584 |
|
| dc.description |
Copyright © by The American Society for Biochemistry and Molecular Biology |
|
| dc.description |
Mammalian AMP-activated protein kinase (AMPK) is a serine/threonine protein kinase that acts as a sensor of cellular energy status. AMPK is a heterotrimer of three different subunits, i.e. α, β and γ, with α being the catalytic subunit and β and γ having regulatory roles. Although several studies have defined different domains in α and β involved in the interaction with the other subunits of the complex, little is known about the regions of the γ subunits involved in these interactions. To study this, we have made sequential deletions from the N-termini of the γ subunit isoforms and studied the interactions with α and β subunits, both by two hybrid analysis and by co-immunoprecipitation. Our results suggest that a conserved region of 20-25 amino acids in γ1, γ2 and γ3, immediately N-terminal to the Bateman domains, is required for the formation of a functional, active αβγ complex. This region is required for the interaction with the β subunits. The interaction between the α and γ subunits does not require this region and occurs instead within the Bateman domains of the γ subunit, although the α-γ interaction does appear to stabilize the β-γ interaction. In addition, sequential deletions from the C-termini of the γ subunits indicate that deletion of any of the CBS motifs prevents the formation of a functional complex with the α and β subunits. |
|
| dc.description |
This study was supported by the EXGENESIS Integrated Project (LSHM-CT-2004-005272) funded by the European Commission. Studies in the PS laboratory were also supported by the Spanish Ministry of Education and Science grant SAF2005-00852. Studies in the DGH laboratory were also supported by a Programme Grant from the Wellcome Trust. |
|
| dc.description |
Peer reviewed |
|
| dc.format |
1166196 bytes |
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| dc.format |
application/pdf |
|
| dc.language |
eng |
|
| dc.publisher |
American Society for Biochemistry and Molecular Biology |
|
| dc.rights |
openAccess |
|
| dc.subject |
AMP-activated protein kinase |
|
| dc.subject |
Gamma subunits |
|
| dc.subject |
Protein-protein interaction |
|
| dc.subject |
Two-hybrid analysis |
|
| dc.subject |
Co-immunoprecipitation |
|
| dc.subject |
Bateman domain |
|
| dc.title |
A conserved sequence immediatelly N-terminal to the bateman domains in AMP-activated protein kinase gamma subunits is required for the interaction with the beta subunits |
|
| dc.type |
Artículo |
|