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Mount Sinai Hospital  >
Pawson, Tony >

Please use this identifier to cite or link to this item: http://hdl.handle.net/1807/9435

Title: Phosphorylation of the SHC proteins on tyrosine correlates with the transformation of fibroblasts and erythroblasts by the v-sea tyrosine kinase
Authors: Crowe, AJ
McGlade, J
Pawson, Tony
Hayman, MJ
Keywords: Adaptor Proteins, Signal Transducing
Erythroblasts
Fibroblasts
Oncogene Proteins, Viral
Phospholipase C
Phosphotransferases (Alcohol Group Acceptor)
Proteins
Tyrosine
Issue Date: Feb-1994
Publisher: Nature Publishing Group
Citation: Oncogene. 1994 Feb;9(2):537-44.
Abstract: The S13 avian erythroblastosis viral genome encodes an oncogenic tyrosine kinase, termed env-sea, that is capable of transforming fibroblasts and erythroblasts. Although the tyrosine kinase activity of the env-sea protein has been shown to be necessary for transformation, no substrates for this enzyme have been detected in vivo. Here we demonstrate that the recently described shc proteins are phosphorylated on tyrosine residues in both S13 transformed fibroblasts and erythroblasts. Furthermore, using an S13 temperature sensitive mutant, we show that the phosphorylation of the shc proteins occurs concomitantly with the activation of the tyrosine kinase activity of the env-sea protein. These observations make the phosphorylation of the shc proteins a good candidate for being involved in oncogenic signaling by the env-sea oncoprotein.
URI: http://www.nature.com
http://hdl.handle.net/1807/9435
ISSN: 0950-9232
Appears in Collections:Pawson, Tony
Pawson, Tony

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