Calcium-dependent translocation of S100A11 requires tubulin filaments

Davey, Gabriela E.; Murmann, Petra; Hoechli, Mathias; Tanaka, Toshio; Heizmann, Claus W.

doi:10.1016/s0167-4889(00)00098-7

Cited by 32 publications

(26 citation statements)

References 41 publications

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“…2). Such a model is consistent with recent studies demonstrating Ca 2ϩ -dependent changes in the subcellular distribution of S100A2, S100A4, and S100A6 (Davey et al, 2000;Mandinova, et al, 1998;Mueller et al, 1999). There is no question that binding sites on both S100 proteins and individual target proteins will play a critical role in mediating S100-target protein interactions.…”

Section: Introductionsupporting

confidence: 89%

Molecular mechanisms of S100‐target protein interactions

Zimmer

Sadosky

Weber

2003

Microscopy Res & Technique

142

124

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S100 proteins have no known enzymatic activity and exert their intracellular effects via interaction with and regulation of the activity of other proteins, termed target proteins, in both a Ca(2+)-dependent and Ca(2+)-independent manner. Structural studies have identified the linker region between the two EF-hand Ca(2+) binding domains and the C-terminus as Ca(2+)-dependent target protein binding sites in several S100 family members. In fact, C-terminal aromatic residues are obligatory for interaction of S100A1 with several of its Ca(2+)-dependent target proteins. Pharmacological studies suggest the presence of additional Ca(2+)-dependent binding motifs on some family members. A minimum of seven family members interact with and regulate the activity of aldolase A in a Ca(2+)-independent manner. In the case of S100A1, Ca(2+)-independent target protein interactions utilize a binding motif distinct from the C-terminal Ca(2+)-dependent target protein binding site. Several studies suggest that ionic interactions participate in the interaction of S100 family members with Ca(2+)-independent target proteins. While some target proteins are activated by multiple family members, other target proteins exhibit family member-specific activation, i.e., they are activated by a single family member. As predicted, family member specific interactions appear to be mediated by regions that exhibit the most divergence in amino acid sequence among family members, the linker or "hinge" region and the C terminus. Further specificity in S100-target protein interactions may arise from the different biochemical/biophysical properties of the individual family members, including affinity for metal ions (Ca(2+), Zn(2+), and Cu(2+)), oligomerization properties, heterodimerization, post-translational modifications, and lipid-binding. Delineation of the structural motifs that mediate S100-target protein interactions and determination of the in vivo relevance of these interactions are needed to fully understand the role of S100 proteins in normal and diseased cells.

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Section: Introductionsupporting

confidence: 89%

Molecular mechanisms of S100‐target protein interactions

Zimmer

Sadosky

Weber

2003

Microscopy Res & Technique

142

124

View full text Add to dashboard Cite

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“…Accordingly, S100A14 exhibited different patterns of subcellular distribution, typified by plasma membrane localization in breast cancer tissues but cytosolic expression in nontumor breast epithelial cells (35). Previous studies showed that some members of the S100 family of proteins exhibit calcium-dependent translocation (36,37), and the translocation of S100A14 is regulated in a calcium-dependent manner through interaction with nucleobindin, which has strong association with Ga proteins (38). We also found that calcium treatment induced S100A14 expression in cell nuclei in esophageal cancer cell lines, further suggesting that calcium plays a role in the induction and translocation of S100A14.…”

Section: Discussionmentioning

confidence: 99%

S100A14: Novel Modulator of Terminal Differentiation in Esophageal Cancer

Chen

Sunkel

et al. 2013

Molecular Cancer Research

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Aberrant keratinocyte differentiation is a key mechanism in the initiation of cancer. Because activities regulating differentiation exhibit altered or reduced capacity in esophageal cancer cells, it is vital to pinpoint those genes that control epidermal proliferation and terminal differentiation to better understand esophageal carcinogenesis. S100A14 is a member of the S100 calcium-binding protein family and has been suggested to be involved in cell proliferation, apoptosis, and invasion. The present study used immunohistochemistry analysis of S100A14 in clinical specimens of esophageal squamous cell carcinoma (ESCC) to show that decreased S100A14 is strongly correlated with poor differentiation. Furthermore, both mRNA and protein expression of S100A14 was drastically increased upon 12-O-tetra-decanoylphorbol-13-acetate (TPA) and calcium-induced esophageal cancer cell differentiation. Overexpression of S100A14 resulted in a G 1 -phase cell cycle arrest and promoted calcium-inhibited cell growth. Conversely, decreasing S100A14 expression significantly promoted G 1 -S transition and prevented the morphologic changes associated with calcium-induced cell differentiation. Molecular investigation demonstrated that S100A14 altered the calcium-induced expression of late markers of differentiation, with the most prominent effect on involucrin (IVL) and filaggrin (FLG). Finally, it was determined that S100A14 is transcriptionally regulated by JunB and that S100A14 and JunB status significantly correlated in ESCC tissue. In summary, these data demonstrate that S100A14 is transcriptionally regulated by JunB and involved in ESCC cell differentiation.

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“…Several S100 proteins have been shown to translocate to cytoskeletal elements upon elevation of cytosolic calcium, suggesting that some S100 members have a role in the regulation of cell shape changes, locomotion, and the three-dimensional organization of the cytoskeleton. 20,[33][34][35][36] Preceding studies from our group demonstrated that S100A8/S100A9 complexes promote the formation of MTs in an MT-associated protein-like fashion. It was shown that S100A8/S100A9 bind to tubulin filaments in a calcium-dependent manner, and functional assays demonstrated a role of native S100A8/S100A9 in polymerization and bundling of MTs.…”

Section: Discussionmentioning

confidence: 99%