Identification of annexin II, annexin VI and glyceraldehyde-3-phosphate dehydrogenase as calcyclin-binding proteins in bovine heart
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Identification and characterization of a centrosomal protein, FOR20 as a novel S100A6 target
2017, Biochemical and Biophysical Research CommunicationsCitation Excerpt :The physiological functions of S100A6 were thought to be mediated by interactions with its target proteins [4]. Previous studies using biochemical approaches identified a number of intracellular target proteins for S100A6 including glyceraldehyde-3-phosphate dehydrogenase, annexin II, annexin VI [5], annexin XI [calcyclin-associated protein 50kDa (CAP-50)] [6], caldesmon [7], tropomyosin [8], calponin, CacyBP/SIP (calcyclin-binding protein and siah-1-Interacting Protein) [9,10], Hsp70/Hsp90-organizing protein, kinesin light chain, translocase of outer mitochondrial membrane 70 [11], protein phosphatase 5 (PP5) [12], FK506-binding protein 38 [13], and C-terminus of Hsc70-interacting protein [14], consistent with its primarily cytoplasmic location. However, the extracellular localization of S100A6 was also shown to be important for modulating the viability of neuroblastoma cell line SH-SY5Y via interactions with the receptor for advanced glycation end products, RAGE [15].
Dentin phosphoprotein binds annexin 2 and is involved in calcium transport in rat kidney ureteric bud cells
2013, Journal of Biological ChemistryCitation Excerpt :It is possible that the high concentration of DPP on the column was responsible for DPP displacing the other binding partners of annexin 2. Annexin 2 has been shown to form complexes with other proteins (27, 28, 32–36). As seen in Fig. 2, there are other minor bands present in the elution.
The role of the annexin A2 heterotetramer in vascular fibrinolysis
2011, BloodCitation Excerpt :The S100 proteins are small, often acidic polypeptides of approximately 10 kDa, containing an N-terminal and a C-terminal EF hand separated by a rather unstructured linker region.58 Interactions between some S100 protein family members and ANXA2 have been previously reported, including heterotetramer formation between ANXA2 and S100A4,59 S100A6,60 and S100A1061 as well as interactions between ANXA1 and S100A11,62 ANXAVI and S100A1 or S100B,63 ANXAVI and S100A6,60 and ANXAXI and S100A6.64 In contrast to all other S100 proteins, S100A10 is not regulated by Ca2+ because of amino acid replacements in its Ca2+-binding sites that have left this protein unable to coordinate calcium.
The tumor-associated antigen 90K/Mac-2-binding protein secreted by human colon carcinoma cells enhances extracellular levels of promatrilysin and is a novel substrate of matrix metalloproteinases-2, -7 (matrilysin) and -9: Implications of proteolytic cleavage
2010, Biochimica et Biophysica Acta - General SubjectsBinding of S100 proteins to RAGE: An update
2009, Biochimica et Biophysica Acta - Molecular Cell ResearchS100A6 binds p53 and affects its activity
2009, International Journal of Biochemistry and Cell Biology