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CA2 — GSN

Text-mined interactions from Literome

Takiguchi et al., Cell Struct Funct 2000 : After this phosphorylation, gelsolin no longer requires Ca2+ for activity ; it severs and subsequently caps actin filaments, and nucleates filament formation in Ca2+-free solution
Kiselar et al., Proc Natl Acad Sci U S A 2003 : Visualizing the Ca2+ dependent activation of gelsolin by using synchrotron footprinting
Ashish et al., J Biol Chem 2007 : Global structure changes associated with Ca2+ activation of full-length human plasma gelsolin
Nag et al., Proc Natl Acad Sci U S A 2009 : Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin
Coué et al., J Biol Chem 1985 : Plasma gelsolin formed a very tight 1 : 2 complex with G-actin in the presence of Ca2+ , but no interaction between gelsolin and G-actin was detected in the presence of excess EGTA
Hwo et al., J Cell Biol 1986 : We have purified and characterized monoclonal antibodies that recognize Ca2+ induced conformational changes in human platelet gelsolin (G) and human plasma brevin (B), a closely related protein
Coué et al., J Biol Chem 1986 : In the presence of Ca2+ , gelsolin forms a very tight, stoichiometric complex with 2 molecules of ADP-G-actin
Rouayrenc et al., Biochemistry 1986 : Characterization of the Ca2+ induced conformational changes in gelsolin and identification of interaction regions between actin and gelsolin
Martin et al., Biochem Biophys Res Commun 1987 : Sequence analysis shows that 67 kDa bovine aorta protein shares common domains with p36 and possesses the consensus aminoacid sequences of mammalian Ca2+ dependent membrane binding protein and p36/gelsolin
Brady et al., Nature 1984 : In the presence of EGTA, gelsolin has no effect on the movement of membranous organelles, but in the presence of 10 microM Ca2+ it completely blocks transport of all membranous organelles
Yin et al., J Biol Chem 1980 : In the presence of micromolar Ca2+ , gelsolin bound Ca2+
Hesterkamp et al., Eur J Biochem 1993 : Gelsolin forms ternary complexes with two actin monomers in the presence of Ca2+ , which nucleate actin polymerization and cap the barbed ends of filaments
Lamb et al., J Biol Chem 1993 : At pH below 6.0, gelsolin no longer requires Ca2+ for activity and severs actin filaments, binds two actin monomers, and nucleates filament formation in EGTA containing solutions
Feinberg et al., Biochem J 1993 : The gelsolin-actin complex in the presence of Ca2+ revealed at least three interacting sites on the gelsolin molecule located in the S1, S2-3, and S4-6 domains
Lin et al., J Biol Chem 1997 : Gelsolin and CapG affinity for PIP2 were increased 8- and 4-fold, respectively, by microM Ca2+ , and the Ca2+ requirement was reduced by lowering the pH from 7.5 to 7.0