2024-03-28T09:41:20Zhttp://digital.csic.es/dspace-oai/requestoai:digital.csic.es:10261/1120952019-02-21T10:49:28Zcom_10261_109com_10261_1col_10261_362
AMP-activated protein kinase: structure and regulation.
Sanz, Pascual
AMP-activated protein kinase
Snf1
LKB1
CaMKK
Phosphatase
15 páginas, 5 figuras, 3 tablas
Mammalian AMP-activated protein kinase (AMPK) is a serine/threonine protein kinase that acts as a sensor of cellular energy status. It is activated by a large variety of cellular stresses that increase cellular AMP and decrease ATP levels and also by physiological stimuli, such as muscle contraction, or by hormones such as leptin and adiponectin. AMPK modulates multiple metabolic pathways. As a result, it has become a target for the development of new drugs for the treatment of type II diabetes, obesity or even cancer. In fact, it has been recently reported that drugs used in the treatment of diabetes, such as metformin and thiazolidinediones (TZDs), exert their beneficial effects through the activation of AMPK. AMPK is a heterotrimeric complex composed of a catalytic subunit (AMPK-) and two regulatory subunits (AMPK- and AMPK-). Functional orthologues of this kinase complex are found throughout eukaryotic kingdom, from yeast to humans, indicating that the function of this complex is evolutionarily conserved. This review summarizes the recent studies on the structure and regulation of the AMPK heterotrimeric complex.
This work has been supported by the Research and Technological Development Project LSHM-CT-2004-005272 funded by the European Commission, the Spanish Ministry of Education and Science grant SAF2005-00852 and grants from the CIBER de Enfermedades Raras, an initiative of the ISCIII.
Peer reviewed
2015-03-10T11:51:36Z
2015-03-10T11:51:36Z
2008-10
artículo
http://purl.org/coar/resource_type/c_6501
Current Protein and Peptide Science 9(5):478-92. (2008)
1389-2037
http://hdl.handle.net/10261/112095
10.2174/138920308785915254
1875-5550
en
Postprint
http://dx.doi.org/10.2174/138920308785915254
Sí
open
Bentham Science Publishers