title: ERBB receptors in cancer: signaling from the inside.
abstract: ERBB receptor tyrosine kinases are activated by ligand-induced dimerization followed by activation and transphosphorylation of their intracellular kinase domains. A recent study by Bill and colleagues demonstrates that receptor transphosphorylation can be regulated from inside the cell by members of the cytohesin protein family. These data highlight a novel mechanism of amplification of ERBB receptor signaling output that may contribute to embryogenesis and cancer progression.
authors: Department of Medicine, Vanderbilt-Ingram Cancer Center, Vanderbilt University School of Medicine, Division of Hematology/Oncology, VUMC, 2220 Pierce Avenue, 777 PRB, Nashville, TN 37232-6307, USA. carlos.arteaga@vanderbilt.edu
authors: Carlos L
authors: CL
authors: Arteaga
mesh_terms: D001943:Breast Neoplasms / Q000235:genetics / Q000378:metabolism*; D002454:Cell Differentiation; D002465:Cell Movement; D004789:Enzyme Activation / Q000235:genetics; D066246:ErbB Receptors / Q000378:metabolism*; D005260:Female; D020690:GTPase-Activating Proteins / Q000378:metabolism; D020662:Guanine Nucleotide Exchange Factors / Q000378:metabolism; D006801:Humans; D020794:Receptor Protein-Tyrosine Kinases / Q000235:genetics / Q000378:metabolism*; D015398:Signal Transduction
chemical_list: D020690:GTPase-Activating Proteins; D020662:Guanine Nucleotide Exchange Factors; C100723:cytohesin-1; C102474:cytohesin-2; C512478:EGFR protein, human; D066246:ErbB Receptors; D020794:Receptor Protein-Tyrosine Kinases