Structure/function studies of lin-12/Notch proteins.
The lin-12/Notch proteins appear to act as transmembrane receptors for intercellular signals that specify cell fates during animal development. Recent structure/function studies have shown that the lin-12/Notch intracellular domain alone has the intrinsic signal-transducing activity of the intact protein, and that the role of the extracellular domain is to regulate this intrinsic activity. These studies have also suggested that the different lin-12/Notch proteins in a given organism are interchangeable biochemically and have addressed the role of lin-12/Notch genes in development.
Greenwald
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Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biophysics, Columbia University, College of Physicians and Surgeons, New York, New York 10032.
D000595:Amino Acid Sequence; D000818:Animals; D017089:Ankyrin Repeat; D017173:Caenorhabditis elegans / Q000196:embryology / Q000235:genetics; D029742:Caenorhabditis elegans Proteins; D004330:Drosophila / Q000196:embryology / Q000235:genetics; D029721:Drosophila Proteins; D004627:Embryonic Induction / Q000235:genetics*; D018507:Gene Expression Regulation, Developmental; D015801:Helminth Proteins / Q000737:chemistry / Q000502:physiology; D006801:Humans; D007301:Insect Hormones / Q000737:chemistry / Q000502:physiology*; D008565:Membrane Proteins / Q000737:chemistry / Q000502:physiology*; D005810:Multigene Family; D051880:Receptors, Notch; D015398:Signal Transduction / Q000502:physiology*; D013329:Structure-Activity Relationship
D029742:Caenorhabditis elegans Proteins; D029721:Drosophila Proteins; D015801:Helminth Proteins; D007301:Insect Hormones; C082460:Lin-12 protein, C elegans; D008565:Membrane Proteins; C497759:N protein, Drosophila; D051880:Receptors, Notch