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ANXA1 — CA2

Text-mined interactions from Literome

Edashige et al., Arch Biochem Biophys 1992 : Annexin I required Ca2+ for both its association with phospholipid membranes and phosphorylation by PKC, whereas histone and monomyristilated lysozyme ( C14 : 0-lysozyme ) did not
Dorovkov et al., J Biol Chem 2004 : Phosphorylation of annexin 1 by TRPM7 kinase is stimulated by Ca2+ and is dramatically increased in extracts from cells overexpressing TRPM7
McNeil et al., J Biol Chem 2006 : We propose that Ca2+ entering through a disruption locally induces annexin A1 binding to membranes, initiating emergency fusion events whenever and wherever required
Hayashi et al., Biochem J 1990 : Lipocortin I required greater than or equal to 10 microM-Ca2+ to bind the two antibodies, and this Ca2+ requirement was not affected by phosphatidylserine
Schlaepfer et al., J Biol Chem 1987 : Characterization of Ca2+ dependent phospholipid binding and phosphorylation of lipocortin I ... Lipocortin I associated with phosphatidylserine vesicles and F-actin in a Ca2+ dependent manner with half-maximal association occurring at 22 and 180 microM Ca2+, respectively ... Phosphorylation of lipocortin I by the epidermal growth factor stimulated kinase in A431 membranes required Ca2+ ( half-maximum = 28 microM ) in the presence of Mg2+, but phosphorylation was not Ca2+ dependent in the presence of Mn2+
Haigler et al., J Biol Chem 1987 : However, both the unidentified protein, lipocortin I, and 32P labeled lipocortin I bound in a Ca2+ dependent manner to the [ 3H ] oleic acid labeled Escherichia coli membranes used as substrate in the phospholipase A2 assay
Eldering et al., FEBS Lett 1993 : Without detergents, when resting platelets were lysed and fractionated in the absence of Ca2+, lipocortin I was found only in the cytosolic fraction, whereas, in the presence of Ca2+ , lipocortin I was associated only with the crude particulate and not with the membrane nor the cytosolic fractions
Katoh et al., Lipids 1996 : The enhanced phosphorylation of annexin I by GT1b was also dependent on PS and Ca2+ ... These results suggest that an enzyme or enzymes other than protein kinase C, epidermal growth factor receptor kinase, or insulin receptor kinase is responsible for the GT1b- and GD3 enhanced phosphorylation of annexin I in the presence of PS and Ca2+
Seemann et al., Mol Biol Cell 1996 : The association of annexin I with early endosomes is regulated by Ca2+ and requires an intact N-terminal domain
Allen et al., Biochem Cell Biol 1996 : Calgizzarin is a Ca2+ binding protein of the S100 family that has been implicated in the regulation of cytoskeletal function through its Ca2+ dependent interaction with annexin I
Bitto et al., Biochemistry 1998 : When the cap residues of type II Ca2+ binding sites were systematically mutated to Ala, a type II site in domain II was shown to be essential for Ca2+ dependent vesicle binding of annexin I
Lee et al., FEBS Lett 1999 : The interaction between ANX1 and ANX2 also occurred in vitro in a Ca2+ dependent manner