FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1997894911> ?p ?o ?g. }

• W1997894911 endingPage "25764" @default.
• W1997894911 startingPage "25755" @default.
• W1997894911 abstract "Platelet activation triggers integrin αIIbβ3-dependent signals and the induction of tyrosine phosphorylation of the cytoskeletal protein α-actinin. We have previously reported that α-actinin is phosphorylated by the focal adhesion kinase (FAK) (Izaguirre, G., Aguirre, L., Hu, Y.-P., Lee, H. Y., Schlaepfer, D. D., Aneskievich, B. J., and Haimovich, B. (2001) J. Biol. Chem. 276, 28676-28685). In this study, a phosphatase of 68 kDa that dephosphorylated α-actinin in vitro was isolated from platelet lysates by three sequential chromatography steps. The phosphatase was identified as SHP-1 by electrospray tandem mass spectrometry. α-Actinin was dephosphorylated in vitro by recombinant SHP-1 and by SHP-1 immunoprecipitated from unstimulated or thrombin-stimulated platelet lysates. SHP-1 immunoprecipitated from lysates of platelets adherent to fibrinogen, however, failed to dephosphorylate α-actinin. In contrast, the activity of SHP-1 against a synthetic substrate was not affected by the mode of platelet activation. The robust and sustained phosphorylation of α-actinin detected in platelets adherent to fibrinogen thus correlates with a decrease in the activity of SHP-1 toward it. Tyrosine phosphorylation of α-actinin is seen in vanadate-treated COS-7 cells that are co-transfected with α-actinin and wild type FAK. Triple transfection of the cells with cDNAs encoding for α-actinin, FAK, and wild type SHP-1 abolished the phosphorylation of α-actinin. The phosphorylation of FAK, however, was barely affected by the expression of wild type SHP-1. Both α-actinin and FAK were phosphorylated in cells co-expressing α-actinin, FAK, and a catalytic domain mutant (C453S) of SHP-1. These findings establish that SHP-1 can dephosphorylate α-actinin in vitro and in vivo and suggest that SHP-1 may regulate the tethering of receptors to the cytoskeleton and/or the extent of cross-linking of actin filaments in cells such as platelets. Platelet activation triggers integrin αIIbβ3-dependent signals and the induction of tyrosine phosphorylation of the cytoskeletal protein α-actinin. We have previously reported that α-actinin is phosphorylated by the focal adhesion kinase (FAK) (Izaguirre, G., Aguirre, L., Hu, Y.-P., Lee, H. Y., Schlaepfer, D. D., Aneskievich, B. J., and Haimovich, B. (2001) J. Biol. Chem. 276, 28676-28685). In this study, a phosphatase of 68 kDa that dephosphorylated α-actinin in vitro was isolated from platelet lysates by three sequential chromatography steps. The phosphatase was identified as SHP-1 by electrospray tandem mass spectrometry. α-Actinin was dephosphorylated in vitro by recombinant SHP-1 and by SHP-1 immunoprecipitated from unstimulated or thrombin-stimulated platelet lysates. SHP-1 immunoprecipitated from lysates of platelets adherent to fibrinogen, however, failed to dephosphorylate α-actinin. In contrast, the activity of SHP-1 against a synthetic substrate was not affected by the mode of platelet activation. The robust and sustained phosphorylation of α-actinin detected in platelets adherent to fibrinogen thus correlates with a decrease in the activity of SHP-1 toward it. Tyrosine phosphorylation of α-actinin is seen in vanadate-treated COS-7 cells that are co-transfected with α-actinin and wild type FAK. Triple transfection of the cells with cDNAs encoding for α-actinin, FAK, and wild type SHP-1 abolished the phosphorylation of α-actinin. The phosphorylation of FAK, however, was barely affected by the expression of wild type SHP-1. Both α-actinin and FAK were phosphorylated in cells co-expressing α-actinin, FAK, and a catalytic domain mutant (C453S) of SHP-1. These findings establish that SHP-1 can dephosphorylate α-actinin in vitro and in vivo and suggest that SHP-1 may regulate the tethering of receptors to the cytoskeleton and/or the extent of cross-linking of actin filaments in cells such as platelets." @default.
• W1997894911 created "2016-06-24" @default.
• W1997894911 creator A5021905687 @default.
• W1997894911 creator A5040888166 @default.
• W1997894911 creator A5042128422 @default.
• W1997894911 creator A5044733518 @default.
• W1997894911 creator A5053334442 @default.
• W1997894911 creator A5062765426 @default.
• W1997894911 creator A5080821946 @default.
• W1997894911 date "2004-06-01" @default.
• W1997894911 modified "2023-09-29" @default.
• W1997894911 title "The Protein-tyrosine Phosphatase SHP-1 Regulates the Phosphorylation of α-Actinin" @default.
• W1997894911 cites W1491625645 @default.
• W1997894911 cites W1501702588 @default.
• W1997894911 cites W1535696878 @default.
• W1997894911 cites W1547494165 @default.
• W1997894911 cites W155788393 @default.
• W1997894911 cites W1565477787 @default.
• W1997894911 cites W1929023701 @default.
• W1997894911 cites W1970804746 @default.
• W1997894911 cites W1971427516 @default.
• W1997894911 cites W1975464455 @default.
• W1997894911 cites W1993948601 @default.
• W1997894911 cites W1995088117 @default.
• W1997894911 cites W1999202491 @default.
• W1997894911 cites W2012135526 @default.
• W1997894911 cites W2012496083 @default.
• W1997894911 cites W2013268726 @default.
• W1997894911 cites W2018837494 @default.
• W1997894911 cites W2027980005 @default.
• W1997894911 cites W2028691987 @default.
• W1997894911 cites W2029723738 @default.
• W1997894911 cites W2032667632 @default.
• W1997894911 cites W2040980668 @default.
• W1997894911 cites W2042122259 @default.
• W1997894911 cites W2043682382 @default.
• W1997894911 cites W2048127037 @default.
• W1997894911 cites W2049207651 @default.
• W1997894911 cites W2053001031 @default.
• W1997894911 cites W2056104802 @default.
• W1997894911 cites W2058067037 @default.
• W1997894911 cites W2062099855 @default.
• W1997894911 cites W2064540749 @default.
• W1997894911 cites W2072089764 @default.
• W1997894911 cites W2091289978 @default.
• W1997894911 cites W2092354039 @default.
• W1997894911 cites W2093278555 @default.
• W1997894911 cites W2097856283 @default.
• W1997894911 cites W2101073455 @default.
• W1997894911 cites W2109791066 @default.
• W1997894911 cites W2114653456 @default.
• W1997894911 cites W2117737431 @default.
• W1997894911 cites W2122129887 @default.
• W1997894911 cites W2122720918 @default.
• W1997894911 cites W2123938732 @default.
• W1997894911 cites W2125293856 @default.
• W1997894911 cites W2126104631 @default.
• W1997894911 cites W2130708019 @default.
• W1997894911 cites W2130837149 @default.
• W1997894911 cites W2134884900 @default.
• W1997894911 cites W2138766779 @default.
• W1997894911 cites W2141141508 @default.
• W1997894911 cites W2148206240 @default.
• W1997894911 cites W2149667112 @default.
• W1997894911 cites W2149827890 @default.
• W1997894911 cites W2168783089 @default.
• W1997894911 cites W2171179595 @default.
• W1997894911 cites W2172521244 @default.
• W1997894911 cites W2221942573 @default.
• W1997894911 cites W2317626938 @default.
• W1997894911 doi "https://doi.org/10.1074/jbc.m314175200" @default.
• W1997894911 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15070900" @default.
• W1997894911 hasPublicationYear "2004" @default.
• W1997894911 type Work @default.
• W1997894911 sameAs 1997894911 @default.
• W1997894911 citedByCount "38" @default.
• W1997894911 countsByYear W19978949112012 @default.
• W1997894911 countsByYear W19978949112013 @default.
• W1997894911 countsByYear W19978949112015 @default.
• W1997894911 countsByYear W19978949112016 @default.
• W1997894911 countsByYear W19978949112017 @default.
• W1997894911 countsByYear W19978949112020 @default.
• W1997894911 countsByYear W19978949112021 @default.
• W1997894911 crossrefType "journal-article" @default.
• W1997894911 hasAuthorship W1997894911A5021905687 @default.
• W1997894911 hasAuthorship W1997894911A5040888166 @default.
• W1997894911 hasAuthorship W1997894911A5042128422 @default.
• W1997894911 hasAuthorship W1997894911A5044733518 @default.
• W1997894911 hasAuthorship W1997894911A5053334442 @default.
• W1997894911 hasAuthorship W1997894911A5062765426 @default.
• W1997894911 hasAuthorship W1997894911A5080821946 @default.
• W1997894911 hasBestOaLocation W19978949111 @default.
• W1997894911 hasConcept C11960822 @default.
• W1997894911 hasConcept C153911025 @default.
• W1997894911 hasConcept C178666793 @default.
• W1997894911 hasConcept C185592680 @default.
• W1997894911 hasConcept C203014093 @default.
• W1997894911 hasConcept C2776165026 @default.

• next