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• W185372314 abstract "The signal transduction field has recently seen a surge of interest in cascade scaffolding proteins. One of these, the Kinase Suppressor of Ras (KSR), has received a great deal of attention as a scaffold for the Ras/ERK signaling pathway. KSR interacts with both MEK and ERK, and possibly binds to Raf-1 as well. Very little is known about the regulation of KSR; however, it has been determined that membrane association is essential for its function in signal augmentation. KSR shares a high degree of sequence homology to Raf-1, including an almost identical phosphatidic acid binding region (PABR). Previous work in the Romero lab has determined the direct interaction of Raf-1 with phosphatidic acid is critical for its membrane recruitment. The PABR is a 35 amino acid sequence consisting of a poly-basic motif (PBM) flanked by two hydrophobic regions. Neutralization of the two arginine residues in the PBM abrogates the binding of Raf-1 to phosphatidic acid (PA), and consequently disrupts its membrane association. This thesis examines lipid-binding properties of the PABR and their potential role in the traffic and function of KSR. Using peptides corresponding to the PABR and tryptophan fluorescence spectroscopy, the data presented in the first section demonstrate that PA induces a blue-shift in the tryptophan emission spectra of WT KSR PABR, and this shift is specific for PA. The second section explores the cellular consequence of KSR PABR mutation. A KSR protein lacking the arginine residues in the PBM expressed in HIRcB fibroblasts retains its membrane-binding ability, but inhibits MEK and ERK phosphorylation in a dominant negative fashion. The data presented here support the conclusion that, although an intact PABR may not be essential for the membrane localization of KSR, it is essential for proper coupling of the pathway." @default.
• W185372314 created "2016-06-24" @default.
• W185372314 creator A5016918385 @default.
• W185372314 date "2005-12-09" @default.
• W185372314 modified "2023-09-27" @default.
• W185372314 title "Lipid binding and the scaffolding function of the Kinase Suppressor of Ras" @default.
• W185372314 cites W1489297798 @default.
• W185372314 cites W1587627449 @default.
• W185372314 cites W1853445387 @default.
• W185372314 cites W1876564982 @default.
• W185372314 cites W1969405246 @default.
• W185372314 cites W1972812612 @default.
• W185372314 cites W1978535713 @default.
• W185372314 cites W1978760124 @default.
• W185372314 cites W1979008438 @default.
• W185372314 cites W1983728585 @default.
• W185372314 cites W1984536659 @default.
• W185372314 cites W1984906223 @default.
• W185372314 cites W1985427839 @default.
• W185372314 cites W1992117451 @default.
• W185372314 cites W1992643136 @default.
• W185372314 cites W1993385052 @default.
• W185372314 cites W1994772914 @default.
• W185372314 cites W1995685525 @default.
• W185372314 cites W1997388514 @default.
• W185372314 cites W2002127663 @default.
• W185372314 cites W2007665864 @default.
• W185372314 cites W2008333101 @default.
• W185372314 cites W2008346251 @default.
• W185372314 cites W2010994547 @default.
• W185372314 cites W2011184275 @default.
• W185372314 cites W2011185477 @default.
• W185372314 cites W2011221649 @default.
• W185372314 cites W2015851233 @default.
• W185372314 cites W2016235845 @default.
• W185372314 cites W2020257412 @default.
• W185372314 cites W2026593149 @default.
• W185372314 cites W2040585305 @default.
• W185372314 cites W2043775652 @default.
• W185372314 cites W2047962409 @default.
• W185372314 cites W2049513608 @default.
• W185372314 cites W2052122921 @default.
• W185372314 cites W2056857208 @default.
• W185372314 cites W2057392977 @default.
• W185372314 cites W2059672480 @default.
• W185372314 cites W2060224232 @default.
• W185372314 cites W2060630008 @default.
• W185372314 cites W2060840912 @default.
• W185372314 cites W2066113694 @default.
• W185372314 cites W2068033067 @default.
• W185372314 cites W2069431286 @default.
• W185372314 cites W2069883690 @default.
• W185372314 cites W2070808893 @default.
• W185372314 cites W2072243374 @default.
• W185372314 cites W2072318475 @default.
• W185372314 cites W2073131401 @default.
• W185372314 cites W2074303585 @default.
• W185372314 cites W2077086907 @default.
• W185372314 cites W2078522456 @default.
• W185372314 cites W2079618910 @default.
• W185372314 cites W2085931606 @default.
• W185372314 cites W2086386747 @default.
• W185372314 cites W2086419819 @default.
• W185372314 cites W2086741479 @default.
• W185372314 cites W2087095360 @default.
• W185372314 cites W2087147037 @default.
• W185372314 cites W2087806196 @default.
• W185372314 cites W2094304273 @default.
• W185372314 cites W2096248361 @default.
• W185372314 cites W2099267053 @default.
• W185372314 cites W2101417059 @default.
• W185372314 cites W2101704246 @default.
• W185372314 cites W2105298978 @default.
• W185372314 cites W2107457780 @default.
• W185372314 cites W2109659042 @default.
• W185372314 cites W2111525938 @default.
• W185372314 cites W2112879240 @default.
• W185372314 cites W2115142313 @default.
• W185372314 cites W2116669977 @default.
• W185372314 cites W2117695239 @default.
• W185372314 cites W2136623592 @default.
• W185372314 cites W2136627244 @default.
• W185372314 cites W2142242441 @default.
• W185372314 cites W2146173859 @default.
• W185372314 cites W2149242879 @default.
• W185372314 cites W2151542719 @default.
• W185372314 cites W2151981938 @default.
• W185372314 cites W2156433178 @default.
• W185372314 cites W2158730778 @default.
• W185372314 cites W2159422521 @default.
• W185372314 cites W2165608776 @default.
• W185372314 cites W2166077873 @default.
• W185372314 cites W2166731355 @default.
• W185372314 cites W2171859557 @default.
• W185372314 cites W2187989464 @default.
• W185372314 cites W2337225223 @default.
• W185372314 cites W38887874 @default.
• W185372314 cites W1986229370 @default.
• W185372314 hasPublicationYear "2005" @default.
• W185372314 type Work @default.

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