S100 protein–annexin interactions: a model of the (Anx2-p11)2 heterotetramer complex

Santos, Jana Sopková−de Oliveira; Oling, Frank; Réty, S.; Brisson, Alain; Smith, Jeremy C.; Lewit-Bentley, Anita

doi:10.1016/s0167-4889(00)00095-1

Cited by 25 publications

(21 citation statements)

References 21 publications

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“…Several annexins are also known to interact and form complexes with S100 proteins (e.g. annexin 1 with S100A11, annexin 2 with S100A10, and S100A4, and annexin 4 and annexin 11 with S100A6) [40]. Annexins A2, A4, A5, A6, A7 and A11 were all detected with increased expression levels in cisplatin resistant HeLa cells.…”

Section: Discussionmentioning

confidence: 99%

Quantitative Proteomic and Interaction Network Analysis of Cisplatin Resistance in HeLa Cells

et al. 2011

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Cisplatin along with other platinum based drugs are some of the most widely used chemotherapeutic agents. However drug resistance is a major problem for the successful chemotherapeutic treatment of cancer. Current evidence suggests that drug resistance is a multifactorial problem due to changes in the expression levels and activity of a wide number of proteins. A majority of the studies to date have quantified mRNA levels between drug resistant and drug sensitive cell lines. Unfortunately mRNA levels do not always correlate with protein expression levels due to post-transcriptional changes in protein abundance. Therefore global quantitative proteomics screens are needed to identify the protein targets that are differentially expressed in drug resistant cell lines. Here we employ a quantitative proteomics technique using stable isotope labeling with amino acids in cell culture (SILAC) coupled with mass spectrometry to quantify changes in protein levels between cisplatin resistant (HeLa/CDDP) and sensitive HeLa cells in an unbiased fashion. A total of 856 proteins were identified and quantified, with 374 displaying significantly altered expression levels between the cell lines. Expression level data was then integrated with a network of protein-protein interactions, and biological pathways to obtain a systems level view of proteome changes which occur with cisplatin resistance. Several of these proteins have been previously implicated in resistance towards platinum-based and other drugs, while many represent new potential markers or therapeutic targets.

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Section: Discussionmentioning

confidence: 99%

Quantitative Proteomic and Interaction Network Analysis of Cisplatin Resistance in HeLa Cells

et al. 2011

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“…In the S100 proteins the domain-domain interactions occur through homo-or hetero-dimerization. [77][78][79][80][81] A compact arrangement of four EF-hands reminiscent of parvalbumins is found in the invertebrate sarcoplasmic calcium-binding proteins. 82,83 In recoverin 84,86 and related four EF-hand proteins from the group termed neuronal calcium sensors (NCS) including frequenin, 87,88 calcineurin B, 89 CIB1, 46 KChIP1 47 the domains are positioned sideways with respect to each other, which creates an extensive hydrophobic surface.…”

Section: The Two-ef-hand Domain As a Functional Unitmentioning

confidence: 99%

Structural Basis for Diversity of the EF-hand Calcium-binding Proteins

Grabarek

2006

Journal of Molecular Biology

343

369

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“…In this regard, it has been proposed that charged residues in individual monomers of an S100 dimers might play a role in the stabilization of heterocomplexes made of two copies of an S100 protein plus two copies of target protein (Garbuglia et al 2000;Sopkova-de Oliveira Santos et al, 2000). There is consensus that, within cells, S100 proteins serve the function of regulating the activity of effector proteins.…”

Section: Introductionmentioning

confidence: 99%

Intracellular and extracellular roles of S100 proteins

Donato

2003

Microscopy Res & Technique

860

725

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S100, a multigenic family of non-ubiquitous Ca(2+)-modulated proteins of the EF-hand type expressed in vertebrates exclusively, has been implicated in intracellular and extracellular regulatory activities. Members of this protein family have been shown to interact with several effector proteins within cells thereby regulating enzyme activities, the dynamics of cytoskeleton constituents, cell growth and differentiation, and Ca(2+) homeostasis. Structural information indicates that most of S100 proteins exist in the form of antiparallelly packed homodimers (in some cases heterodimers), capable of functionally crossbridging two homologous or heterologous target proteins in a Ca(2+)-dependent (and, in some instances, Ca(2+)-independent) manner. In addition, extracellular roles have been described for several S100 members, although secretion (via an unknown mechanism) has been documented for a few of them. Extracellular S100 proteins have been shown to exert regulatory effects on inflammatory cells, neurons, astrocytes, microglia, and endothelial and epithelial cells, and a cell surface receptor, RAGE, has been identified as a potential S100A12 and S100B receptor transducing the effects of these two proteins on inflammatory cells and neurons. Other cell surface molecules with ability to interact with S100 members have been identified, suggesting that RAGE might not be a universal S100 protein receptor and/or that a single S100 protein might interact with more than one receptor. Collectively, these data indicate that members of the S100 protein family are multifunctional proteins implicated in the regulation of a variety of cellular activities.

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S100 protein–annexin interactions: a model of the (Anx2-p11)2 heterotetramer complex

Cited by 25 publications

References 21 publications

Quantitative Proteomic and Interaction Network Analysis of Cisplatin Resistance in HeLa Cells

Quantitative Proteomic and Interaction Network Analysis of Cisplatin Resistance in HeLa Cells

Structural Basis for Diversity of the EF-hand Calcium-binding Proteins

Intracellular and extracellular roles of S100 proteins

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