Disruption of acl-4, an evolutionarily conserved acyltransferase-like gene, causes synergistic movement defects under polyunsaturated fatty acids depleted condition in C.elegans Export

@inproceedings{citeulike:3327154, abstract = {Phospholipids are the major constituents of cell membranes, and proposed to have numerous structural and functional roles in vivo. It is generally accepted that various phospholipid molecular species are formed by phospholipid acyltransferase reactions; however, their physiological significance and the enzymes responsible for the reactions are largely unknown. To address these questions, we focused on evolutionarily conserved acyltransferase-like genes in C.elegans (named acl-1\~{}14), and isolated their deletion mutants by using TMP / UV method. The mutants of acl-4, which is predominantly expressed in neurons and muscles, showed no apparent phenotype. Since acl genes are assumed to encode acyltransferases, which transfer fatty acyl chains into phospholipid precursors, we analyzed the acl-4 mutants in fat mutant backgrounds in which fatty acid compositions are altered. Interestingly, we found that acl-4 mutants show severe movement abnormalities under polyunsaturated fatty acids depleted conditions (fat-3mutant background). The locomotion rate of acl-4;fat-3 mutants was much slower than that of acl-4 or fat-3 single mutants, and the normal sinusoidal movement pattern was impaired. Pharmacological studies using levamisole and aldicarb revealed that presynaptic activities were slightly reduced in acl-4;fat-3 mutants. These defects were rescued by neuron specific expression of acl-4, suggesting that acl-4 functions in neurons to support the normal locomotion.}, author = {Hara, Naoko and Inoue, Takao and Arai, Hiroyuki}, citeulike-article-id = {3327154}, citeulike-linkout-0 = {http://www.wormbase.org/db/misc/paper?name=WBPaper00028690}, keywords = {acl-4, c\_elegans, caenorhabditis\_elegans, celegans, elegans, f49h126, fat-3, meeting\_abstract, nematode, w08d24, wormbase}, posted-at = {2008-09-24 03:21:37}, priority = {3}, title = {Disruption of acl-4, an evolutionarily conserved acyltransferase-like gene, causes synergistic movement defects under polyunsaturated fatty acids depleted condition in C.elegans}, url = {http://www.wormbase.org/db/misc/paper?name=WBPaper00028690} }

TY - CONF ID - citeulike:3327154 L3 - citeulike-article-id:3327154 N2 - Phospholipids are the major constituents of cell membranes, and proposed to have numerous structural and functional roles in vivo. It is generally accepted that various phospholipid molecular species are formed by phospholipid acyltransferase reactions; however, their physiological significance and the enzymes responsible for the reactions are largely unknown. To address these questions, we focused on evolutionarily conserved acyltransferase-like genes in C.elegans (named acl-1~14), and isolated their deletion mutants by using TMP / UV method. The mutants of acl-4, which is predominantly expressed in neurons and muscles, showed no apparent phenotype. Since acl genes are assumed to encode acyltransferases, which transfer fatty acyl chains into phospholipid precursors, we analyzed the acl-4 mutants in fat mutant backgrounds in which fatty acid compositions are altered. Interestingly, we found that acl-4 mutants show severe movement abnormalities under polyunsaturated fatty acids depleted conditions (fat-3mutant background). The locomotion rate of acl-4;fat-3 mutants was much slower than that of acl-4 or fat-3 single mutants, and the normal sinusoidal movement pattern was impaired. Pharmacological studies using levamisole and aldicarb revealed that presynaptic activities were slightly reduced in acl-4;fat-3 mutants. These defects were rescued by neuron specific expression of acl-4, suggesting that acl-4 functions in neurons to support the normal locomotion. TI - Disruption of acl-4, an evolutionarily conserved acyltransferase-like gene, causes synergistic movement defects under polyunsaturated fatty acids depleted condition in C.elegans KW - acl-4 KW - c_elegans KW - caenorhabditis_elegans KW - celegans KW - elegans KW - f49h126 KW - fat-3 KW - meeting_abstract KW - nematode KW - w08d24 KW - wormbase AU - Hara, Naoko AU - Inoue, Takao AU - Arai, Hiroyuki UR - http://www.wormbase.org/db/misc/paper?name=WBPaper00028690 ER -