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Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase
We have recently shown that changes in tyrosine phosphorylation of a 130-kDa protein(s) (pp130) may be involved in integrin signaling (Kornberg, L., Earp, H.S., Turner, C., Prokop, and Juliano, R. L. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 8392-8396). One component of the pp130 protein complex reac...
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Published in: | The Journal of biological chemistry 1992-11, Vol.267 (33), p.23439-23442 |
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container_end_page | 23442 |
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container_title | The Journal of biological chemistry |
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creator | KORNBERG, L SHELTON EARP, H THOMAS PARSONS, J SCHALLER, M JULIANO, R. L |
description | We have recently shown that changes in tyrosine phosphorylation of a 130-kDa protein(s) (pp130) may be involved in integrin
signaling (Kornberg, L., Earp, H.S., Turner, C., Prokop, and Juliano, R. L. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 8392-8396).
One component of the pp130 protein complex reacts with an antibody generated against p125fak, which is a focal contact-associated
tyrosine kinase (Schaller, M.D., Borgman, C. A., Cobb, B. S., Vines, R. R., Reynolds, A. B., and Parsons, J. T. (1992) Proc.
Natl. Acad. Sci. U.S.A. 89, 5192-5196). Both antibody-mediated integrin clustering and adhesion of KB cells to fibronectin
leads to increased tyrosine phosphorylation of p125fak. The phosphorylation of p125fak is coincident with adhesion of cells
to fibronectin and is maximal prior to cell spreading. Tyrosine phosphorylation of p125fak is induced when KB cells are allowed
to adhere to fibronectin, collagen type IV, or laminin, but is not induced on polylysine. When KB cells are subjected to indirect
immunofluorescence microscopy, p125fak colocalizes with talin in focal contacts. These data provide additional evidence that
tyrosine kinases are involved in integrin signaling. |
doi_str_mv | 10.1016/s0021-9258(18)35853-8 |
format | article |
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signaling (Kornberg, L., Earp, H.S., Turner, C., Prokop, and Juliano, R. L. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 8392-8396).
One component of the pp130 protein complex reacts with an antibody generated against p125fak, which is a focal contact-associated
tyrosine kinase (Schaller, M.D., Borgman, C. A., Cobb, B. S., Vines, R. R., Reynolds, A. B., and Parsons, J. T. (1992) Proc.
Natl. Acad. Sci. U.S.A. 89, 5192-5196). Both antibody-mediated integrin clustering and adhesion of KB cells to fibronectin
leads to increased tyrosine phosphorylation of p125fak. The phosphorylation of p125fak is coincident with adhesion of cells
to fibronectin and is maximal prior to cell spreading. Tyrosine phosphorylation of p125fak is induced when KB cells are allowed
to adhere to fibronectin, collagen type IV, or laminin, but is not induced on polylysine. When KB cells are subjected to indirect
immunofluorescence microscopy, p125fak colocalizes with talin in focal contacts. These data provide additional evidence that
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signaling (Kornberg, L., Earp, H.S., Turner, C., Prokop, and Juliano, R. L. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 8392-8396).
One component of the pp130 protein complex reacts with an antibody generated against p125fak, which is a focal contact-associated
tyrosine kinase (Schaller, M.D., Borgman, C. A., Cobb, B. S., Vines, R. R., Reynolds, A. B., and Parsons, J. T. (1992) Proc.
Natl. Acad. Sci. U.S.A. 89, 5192-5196). Both antibody-mediated integrin clustering and adhesion of KB cells to fibronectin
leads to increased tyrosine phosphorylation of p125fak. The phosphorylation of p125fak is coincident with adhesion of cells
to fibronectin and is maximal prior to cell spreading. Tyrosine phosphorylation of p125fak is induced when KB cells are allowed
to adhere to fibronectin, collagen type IV, or laminin, but is not induced on polylysine. When KB cells are subjected to indirect
immunofluorescence microscopy, p125fak colocalizes with talin in focal contacts. These data provide additional evidence that
tyrosine kinases are involved in integrin signaling.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Cell Adhesion</subject><subject>Cell Adhesion Molecules - isolation & purification</subject><subject>Cell Adhesion Molecules - metabolism</subject><subject>Cell physiology</subject><subject>Cells, Cultured</subject><subject>Chick Embryo</subject><subject>chickens</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>fibroblasts</subject><subject>Fibroblasts - physiology</subject><subject>fibronectin</subject><subject>Fibronectins - metabolism</subject><subject>Focal Adhesion Kinase 1</subject><subject>Focal Adhesion Protein-Tyrosine Kinases</subject><subject>focal adhesion-associated tyrosine kinase</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>integrin</subject><subject>Integrins - metabolism</subject><subject>KB Cells</subject><subject>Kinetics</subject><subject>mediation</subject><subject>Molecular and cellular biology</subject><subject>Molecular Weight</subject><subject>Phosphorylation</subject><subject>Protein-Tyrosine Kinases - isolation & purification</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>receptors</subject><subject>Signal Transduction</subject><subject>tyrosine</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><recordid>eNqFkU2LFDEQhoMo6-zqT1jIQcQ9tKby1clRBr9gwYMK3kImXT0d7e6MSQ8y_97MB7tHAyFF6nmrqLcIuQX2Fhjod4UxDo3lyrwBcyeUUaIxT8gKmBGNUPDzKVk9IM_JdSm_WD3SwhW5AsmtNmpFpjWOI_XdgCWmmaZM47zgNseZhnFfFqzRtv6FjL5gobshlXrzYfTLSdBTT_sU_GORxpeSQvQLdnQ55FTijPR3nKv-BXnW-7Hgy8t7Q358_PB9_bm5__rpy_r9fROUMksjRZDQGQ7KACIX0nYbKUPbQ7vxyutguDV9UJJxxvpOoOLcotDBSqZlq8QNeX2uu8vpzx7L4qZYQp3Uz5j2xbVCAK8e_BcELTUHAxVUZzDUgUrG3u1ynHw-OGDuuA_37Wi2O5rtwLjTPpyputtLg_1mwu5RdV5Azb-65H2pJvbZzyGWB0xK3dpT-ws2xO3wN2Z0m5jCgJPjunVCuGqSsOIfCa2ftA</recordid><startdate>19921125</startdate><enddate>19921125</enddate><creator>KORNBERG, L</creator><creator>SHELTON EARP, H</creator><creator>THOMAS PARSONS, J</creator><creator>SCHALLER, M</creator><creator>JULIANO, R. L</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19921125</creationdate><title>Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase</title><author>KORNBERG, L ; SHELTON EARP, H ; THOMAS PARSONS, J ; SCHALLER, M ; JULIANO, R. L</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c558t-43c41d821581ee2349db44c7f17ba5a6c8298fc540200fd3e5229e36c94064753</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Cell Adhesion</topic><topic>Cell Adhesion Molecules - isolation & purification</topic><topic>Cell Adhesion Molecules - metabolism</topic><topic>Cell physiology</topic><topic>Cells, Cultured</topic><topic>Chick Embryo</topic><topic>chickens</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>fibroblasts</topic><topic>Fibroblasts - physiology</topic><topic>fibronectin</topic><topic>Fibronectins - metabolism</topic><topic>Focal Adhesion Kinase 1</topic><topic>Focal Adhesion Protein-Tyrosine Kinases</topic><topic>focal adhesion-associated tyrosine kinase</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>integrin</topic><topic>Integrins - metabolism</topic><topic>KB Cells</topic><topic>Kinetics</topic><topic>mediation</topic><topic>Molecular and cellular biology</topic><topic>Molecular Weight</topic><topic>Phosphorylation</topic><topic>Protein-Tyrosine Kinases - isolation & purification</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>receptors</topic><topic>Signal Transduction</topic><topic>tyrosine</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>KORNBERG, L</creatorcontrib><creatorcontrib>SHELTON EARP, H</creatorcontrib><creatorcontrib>THOMAS PARSONS, J</creatorcontrib><creatorcontrib>SCHALLER, M</creatorcontrib><creatorcontrib>JULIANO, R. L</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>KORNBERG, L</au><au>SHELTON EARP, H</au><au>THOMAS PARSONS, J</au><au>SCHALLER, M</au><au>JULIANO, R. L</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-11-25</date><risdate>1992</risdate><volume>267</volume><issue>33</issue><spage>23439</spage><epage>23442</epage><pages>23439-23442</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>We have recently shown that changes in tyrosine phosphorylation of a 130-kDa protein(s) (pp130) may be involved in integrin
signaling (Kornberg, L., Earp, H.S., Turner, C., Prokop, and Juliano, R. L. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 8392-8396).
One component of the pp130 protein complex reacts with an antibody generated against p125fak, which is a focal contact-associated
tyrosine kinase (Schaller, M.D., Borgman, C. A., Cobb, B. S., Vines, R. R., Reynolds, A. B., and Parsons, J. T. (1992) Proc.
Natl. Acad. Sci. U.S.A. 89, 5192-5196). Both antibody-mediated integrin clustering and adhesion of KB cells to fibronectin
leads to increased tyrosine phosphorylation of p125fak. The phosphorylation of p125fak is coincident with adhesion of cells
to fibronectin and is maximal prior to cell spreading. Tyrosine phosphorylation of p125fak is induced when KB cells are allowed
to adhere to fibronectin, collagen type IV, or laminin, but is not induced on polylysine. When KB cells are subjected to indirect
immunofluorescence microscopy, p125fak colocalizes with talin in focal contacts. These data provide additional evidence that
tyrosine kinases are involved in integrin signaling.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1429685</pmid><doi>10.1016/s0021-9258(18)35853-8</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals Biological and medical sciences Blotting, Western Cell Adhesion Cell Adhesion Molecules - isolation & purification Cell Adhesion Molecules - metabolism Cell physiology Cells, Cultured Chick Embryo chickens Electrophoresis, Polyacrylamide Gel fibroblasts Fibroblasts - physiology fibronectin Fibronectins - metabolism Focal Adhesion Kinase 1 Focal Adhesion Protein-Tyrosine Kinases focal adhesion-associated tyrosine kinase Fundamental and applied biological sciences. Psychology Humans integrin Integrins - metabolism KB Cells Kinetics mediation Molecular and cellular biology Molecular Weight Phosphorylation Protein-Tyrosine Kinases - isolation & purification Protein-Tyrosine Kinases - metabolism receptors Signal Transduction tyrosine |
title | Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase |
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