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MINIREVIEW

5'-AMP-Activated Protein Kinase Signaling in Caenorhabditis elegans

Department of Cell Biology and Biochemistry, Texas Tech University Health Sciences Center, Lubbock, Texas 79430

To whom requests for reprints should be addressed at ¹ Cell Biology & Biochemistry, Mail Stop 6540, 3601 4th Street, TTUHSC, Lubbock, Texas 79430. E-mail: elmus.beale{at}ttuhsc.edu

5'-AMP-activated protein kinase (AMPK) has been called "the metabolic master switch" because of its central role in regulating fuel homeostasis. AMPK, a heterotrimeric serine/threonine protein kinase composed of , β, and subunits, is activated by upstream kinases and by 5'-AMP in response to various nutritional and stress signals. Downstream effects include regulation of metabolism, protein synthesis, cell growth, and mediation of the actions of a number of hormones, including leptin. However, AMPK research represents a young and growing field; hence, there are many unanswered questions regarding the control and action of AMPK. This review presents evidence for the existence of AMPK signaling pathways in Caenorhabditis elegans, a genetically tractable model organism that has yet to be fully exploited to elucidate AMPK signaling mechanisms.

Key Words: AMPK • Caenorhabditis elegans • signaling • model systems • genetics