2006
DOI: 10.1021/bi061754e
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Insights into S100 Target Specificity Examined by a New Interaction between S100A11 and Annexin A2

Abstract: S100 proteins are a group of EF-hand calcium-signaling proteins, many of which interact with members of the calcium- and phospholipid-binding annexin family of proteins. This calcium-sensitive interaction enables two neighboring membrane surfaces, complexed to different annexin proteins, to be brought into close proximity for membrane reorganization, using the S100 protein as a bridging molecule. S100A11 and S100A10 are two members of the S100 family found to interact with the N-termini of annexins A1 and A2, … Show more

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Cited by 52 publications
(68 citation statements)
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“…Instead, ANXA2 colocalized with S100A11 at the injury site and their presence at the repair site was mutually dependent. This is in line with the reported fivefold tighter Ca 2+ -dependent in vitro interaction of S100A11 with ANXA2 as compared with ANXA1 [45] . Our data demonstrate that the key function of S100A11-ANXA2 complex in PMR is to aid in remodeling of actin cytoskeleton at the site of injury to facilitate repair and excision of the damaged cell membrane [1] .…”
Section: Anxa2 and S100a11 In The Pmr Response Of Cancer Cellssupporting
confidence: 91%
“…Instead, ANXA2 colocalized with S100A11 at the injury site and their presence at the repair site was mutually dependent. This is in line with the reported fivefold tighter Ca 2+ -dependent in vitro interaction of S100A11 with ANXA2 as compared with ANXA1 [45] . Our data demonstrate that the key function of S100A11-ANXA2 complex in PMR is to aid in remodeling of actin cytoskeleton at the site of injury to facilitate repair and excision of the damaged cell membrane [1] .…”
Section: Anxa2 and S100a11 In The Pmr Response Of Cancer Cellssupporting
confidence: 91%
“…These EF-hand Ca 2+ -binding proteins are best known as mediators of intracellular Ca 2+ signals, although they are also exported from the cell by a yet unknown mechanism (29). S100 proteins have an exposed hydrophobic binding pocket that mediates protein-protein interactions (30)(31)(32). Additionally, all S100 proteins are minimally homodimeric but some heterodimerize (33) and many appear to form higher order homo-and hetero-oligomers (34,35).…”
mentioning
confidence: 99%
“…For instance, S100A11 translocates from the cytoplasm to the nucleus where it regulates cell proliferation in response to DNA damage (Gorsler et al 2010). S100A11 also interacts with annexin II which has been associated with many cancer (Diaz et al 2004;Emoto et al 2001;Esposito et al 2006;Rintala-Dempsey et al 2006). S100A11 binds to p53 and to the DNA repair protein Rad54B as well (FernandezFernandez, Rutherford, and Fersht 2008;Murzik et al 2008).…”
Section: S100a6mentioning
confidence: 99%