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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5625
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pubmed:dateCreated |
2003-6-6
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pubmed:abstractText |
Cells migrating directionally toward a chemoattractant source display a highly polarized cytoskeletal organization, with F-actin localized predominantly at the anterior and myosin II at the lateral and posterior regions. Dictyostelium discoideum has proven a useful system for elucidating signaling pathways that regulate this chemotactic response. During development, extracellular adenosine 3', 5' monophosphate (cAMP) functions as a primary signal to activate cell surface cAMP receptors (cARs). These receptors transduce different signals depending on whether or not they are coupled to heterotrimeric guanine nucleotide-binding proteins (G proteins) (see the STKE Connections Maps). Multiple G protein-stimulated pathways interact to establish polarity in chemotaxing D. discoideum cells by localizing F-actin at their leading edge and by regulating the phosphorylation state and assembly of myosin II. Many of the molecular interactions described are fundamental to the regulation of chemotaxis in other eukaryotic cells.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic GMP,
http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Cyclase,
http://linkedlifedata.com/resource/pubmed/chemical/Heterotrimeric GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin Type II,
http://linkedlifedata.com/resource/pubmed/chemical/PTEN Phosphohydrolase,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoric Monoester Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Protozoan Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
6
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pubmed:volume |
300
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1525-7
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:12791977-Actins,
pubmed-meshheading:12791977-Animals,
pubmed-meshheading:12791977-Cell Polarity,
pubmed-meshheading:12791977-Chemotaxis,
pubmed-meshheading:12791977-Cyclic AMP,
pubmed-meshheading:12791977-Cyclic GMP,
pubmed-meshheading:12791977-Dictyostelium,
pubmed-meshheading:12791977-Guanylate Cyclase,
pubmed-meshheading:12791977-Heterotrimeric GTP-Binding Proteins,
pubmed-meshheading:12791977-Myosin Type II,
pubmed-meshheading:12791977-PTEN Phosphohydrolase,
pubmed-meshheading:12791977-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:12791977-Phosphoric Monoester Hydrolases,
pubmed-meshheading:12791977-Phosphorylation,
pubmed-meshheading:12791977-Protozoan Proteins,
pubmed-meshheading:12791977-Pseudopodia,
pubmed-meshheading:12791977-Receptors, Cyclic AMP,
pubmed-meshheading:12791977-Signal Transduction,
pubmed-meshheading:12791977-Tumor Suppressor Proteins
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pubmed:year |
2003
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pubmed:articleTitle |
The signal to move: D. discoideum go orienteering.
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pubmed:affiliation |
Laboratory of Cellular and Developmental Biology, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, MD 20892, USA.
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pubmed:publicationType |
Journal Article
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