Millipore Applications Bibliography |
pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions. | ||
| Authors: | Schaller, M D, et al. | |
| Citation: | Proc. Natl. Acad. Sci. U.S.A., 89: 5192-6 (1992) | |
| Pub Med ID: | 1594631 | |
| Year: | 1992 | |
| Abstract: | Expression of the Rous sarcoma virus-encoded oncoprotein, pp60v-src, subverts the normal regulation of cell growth, which results in oncogenic transformation. This process requires the intrinsic protein-tyrosine kinase activity of pp60v-src and is associated with an increase in tyrosine phosphorylation of a number of cellular proteins, candidate substrates for pp60v-src. We report here the isolation of a cDNA encoding a protein, pp125, that is a major phosphotyrosine-containing protein in untransformed chicken embryo cells and exhibits an increase in phosphotyrosine in pp60v-src-transformed chicken embryo cells. This cDNA encodes a cytoplasmic protein-tyrosine kinase which, based upon its predicted amino acid sequence and structure, is the prototype for an additional family of protein-tyrosine kinases. Immunofluorescence localization experiments show that pp125 is localized to focal adhesions; hence, we suggest the name focal adhesion kinase. | |
Please note: This information is provided to you for technical reference. A reprint of the document cited is available from the publisher or from your local library and is not available from Millipore. For further assistance, please contact Millipore's Technical Services.


