The C. elegans AMP-activated protein kinase AAK-2 is phosphorylated by LKB1 and required for resistance to oxidative stress and for normal motility and foraging behavior. Export

@article{citeulike:3337187, abstract = {AAK-2 is one of two alphaisoforms of the AMP-activated protein kinase in C. elegans, and is involved in life span maintenance, stress responses, and germ cell cycle arrest upon dauer entry. We found that AAK-2 was phosphorylated at threonine 243 in response to paraquat treatment and that this phosphorylation depends on PAR-4, the C. elegans LKB1 homologue. Both aak-2 mutation and par-4 knockdown increased the sensitivity of C. elegans worms to paraquat, and the double deficiency did not further increase sensitivity, indicating that aak-2 and par-4 act in a linear pathway. Both mutations also slowed body bending during locomotion and failed to reduce head oscillation in response to anterior touch. Consistent with this abnormal motility and behavioral response, expression of AAK-2::GFP fusion protein was observed in the ventral cord, some neurons, body wall muscle, pharynx, vulva, somatic gonad, and excretory cell. Our study suggests that AMPK can influence the behavior of C. elegans worms in addition to its well-known function in metabolic control.}, author = {Lee, H. and Cho, J. S. and Lambacher, N. and Lee, J. and Lee, S. J. and Lee, T. H. and Gartner, A. and Koo, H. S.}, citeulike-article-id = {3337187}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/18408008}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=18408008}, citeulike-linkout-2 = {http://www.wormbase.org/db/misc/paper?name=WBPaper00031692}, journal = {J Biol Chem}, keywords = {aak-1, aak-2, c\_elegans, caenorhabditis\_elegans, celegans, elegans, nematode, other, par-4, par23, t01c81, wormbase, y59a8b14}, posted-at = {2008-09-25 16:57:37}, priority = {3}, title = {The C. elegans AMP-activated protein kinase AAK-2 is phosphorylated by LKB1 and required for resistance to oxidative stress and for normal motility and foraging behavior.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/18408008}, year = {2008} }

TY - JOUR ID - citeulike:3337187 L3 - citeulike-article-id:3337187 N2 - AAK-2 is one of two alphaisoforms of the AMP-activated protein kinase in C. elegans, and is involved in life span maintenance, stress responses, and germ cell cycle arrest upon dauer entry. We found that AAK-2 was phosphorylated at threonine 243 in response to paraquat treatment and that this phosphorylation depends on PAR-4, the C. elegans LKB1 homologue. Both aak-2 mutation and par-4 knockdown increased the sensitivity of C. elegans worms to paraquat, and the double deficiency did not further increase sensitivity, indicating that aak-2 and par-4 act in a linear pathway. Both mutations also slowed body bending during locomotion and failed to reduce head oscillation in response to anterior touch. Consistent with this abnormal motility and behavioral response, expression of AAK-2::GFP fusion protein was observed in the ventral cord, some neurons, body wall muscle, pharynx, vulva, somatic gonad, and excretory cell. Our study suggests that AMPK can influence the behavior of C. elegans worms in addition to its well-known function in metabolic control. JF - J Biol Chem TI - The C. elegans AMP-activated protein kinase AAK-2 is phosphorylated by LKB1 and required for resistance to oxidative stress and for normal motility and foraging behavior. KW - aak-1 KW - aak-2 KW - c_elegans KW - caenorhabditis_elegans KW - celegans KW - elegans KW - nematode KW - other KW - par-4 KW - par23 KW - t01c81 KW - wormbase KW - y59a8b14 AU - Lee, H AU - Cho, JS AU - Lambacher, N AU - Lee, J AU - Lee, SJ AU - Lee, TH AU - Gartner, A AU - Koo, HS PY - 2008/// UR - http://view.ncbi.nlm.nih.gov/pubmed/18408008 ER -