Heterodimeric interaction and interfaces of S100A1 and S100P

Wang, Guozheng; Zhang, Shu; Fernig, David G.; Spiller, David G.; Martin-Fernandez, Marisa L.; Zhang, Hongmei; Ding, Yi; Rao, Zihe; Rudland, Philip S.; Barraclough, Roger

doi:10.1042/bj20040142

Cited by 32 publications

(35 citation statements)

References 40 publications

(55 reference statements)

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“…The purified rS100A4, rS100A1 and rNMMHCIIA proteins were immobilized on aminosilane surfaces (Thermo Electron, Basingstoke, UK) and binding assays were carried out as described previously (Rahmoune et al, 1998a, b;Chen et al, 2001;Wang et al, 2004). Binding parameters, k on and k off , were calculated using FastFit software (Affinity Sensors) as previously described (Rahmoune et al, 1998a, b;Chen et al, 2001).…”

Section: Optical Biosensor Assaymentioning

confidence: 99%

Mutually antagonistic actions of S100A4 and S100A1 on normal and metastatic phenotypes

et al. 2004

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Increased levels of the homodimeric calcium-binding protein, S100A4, have been shown to cause a metastatic phenotype in at least three independent model systems of breast cancer and its presence in carcinoma cells has been shown to be associated with a reduction in the survival of patients suffering from a range of different cancers. S100A4 has been shown to interact in vitro with another member of the S100 family of proteins, S100A1. The purpose of the present study was to find out whether S100A1 could affect S100A4 function. Fluorescence resonance energy transfer was used to show the interaction of S100A4 and S100A1 in living cells and the binding affinities between S100A4 and S100A1 were determined using a biosensor. S100A1 reduced the S100A4 inhibition of nonmuscle myosin A self-association and phosphorylation in vitro. S100A1 reduced S100A4 induced motility and growth in soft agar and metastasis in vivo. The results show for the first time that interactions between different S100 proteins can affect cancer-related activity, and that the presence of S100A1 protein in carcinoma cells might modulate the effect of S100A4 on their metastatic abilities.

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Section: Optical Biosensor Assaymentioning

confidence: 99%

Mutually antagonistic actions of S100A4 and S100A1 on normal and metastatic phenotypes

et al. 2004

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“…S100 proteins include at least 20 members involved in the regulation of diverse cellular functions, such as cytoskeletal organization, contraction, differentiation, and transcription. By forming dimers, S100 proteins can functionally link target proteins in a Ca 2+ -dependent (and sometimes in a Ca 2+ -independent) manner (Donato 2003;Wang et al 2004;Wright et al 2005;Santamaria-Kisiel et al 2006). Several in vivo findings support an important role of S100A1 in heart function.…”

Section: S100a1 Is a Camentioning

confidence: 91%

Ca2+ signaling in mouse cardiomyocytes with ablated S100A1 protein

Gusev

Ackermann

Heizmann

et al. 2009

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Abstract. S100A1 is a Ca 2+ -binding protein expressed at high levels in the myocardium. It is thought to modulate the Ca 2+ sensitivity of the sarcoplasmic reticulum (SR) Ca 2+ release channels (ryanodine receptors or RyRs) and its expression has been shown to be down regulated in various heart diseases. In this study we used S100A1 knock-out (KO) mice to investigate the consequences of chronic S100A1 deficiency on Ca 2+ cycling in ventricular cardiomyocytes. Confocal Ca 2+ imaging showed that fieldstimulated KO myocytes had near normal Ca 2+ signaling under control conditions but a blunted response to β-adrenergic stimulation with 1 μmol/l isoproterenol (ISO). Voltage-clamp experiments revealed that S100A1-deficient cardiomyocytes have elevated I Ca under basal conditions. This larger Ca 2+ influx was accompanied by augmented Ca 2+ transients and elevated SR Ca 2+ content, without changes in macroscopic excitation-contraction coupling gain, which suggests impaired fractional Ca 2+ release. Exposure of KO and WT cells to ISO led to similar maximal I Ca . Thus, the stimulation of the I Ca was less pronounced in KO cardiomyocytes, suggesting that changes in basal I Ca could underlie the reduced β-adrenergic response. Taken together, our findings indicate that chronic absence of S100A1 results in enhanced L-type Ca 2+ channel activity combined with a blunted SR Ca 2+ release amplification. These findings may have implications in a variety of cardiac pathologies where abnormal RyR Ca 2+ sensitivity or reduced S100A1 levels have been described.

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“…The divalent cations, Ca 2+ and Zn 2+ , are essential to establish the S100P interactions with ezrin and IQGAP1 as no pulldown is observed in the presence of EGTA (not shown). Because S100P can form heterodimers with S100A1 [21] and S100B forms heterodimers with S100A1 [22], we also analyzed whether S100B is present in the S100P pulldowns. However, we were not able to …”

Section: Identification Of S100p-iqgap1-ezrin Complexesmentioning

confidence: 99%

Ezrin interacts with the scaffold protein IQGAP1 and affects its cortical localization

Nammalwar

Heil

Gerke

2015

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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The cortical cytoskeleton constitutes an important subcellular structure that determines cell shape and regulates cell migration as well as membrane traffic to and from the plasma membrane. Many components of the cortical cytoskeleton have been identified including structural and scaffolding proteins, membrane-cytoskeleton linker proteins and signaling intermediates. We describe here an association of the membrane-F-actin linker protein ezrin with the scaffolding protein IQGAP1 that serves as a hub for concentrating different signaling complexes. Both, ezrin and IQGAP1 bind in a Ca²⁺-dependent manner to the EF hand protein S100P and complexes consisting of Ca²⁺-bound S100P, IQGAP1 and ezrin can be isolated by immunoprecipitation. Ezrin and IQGAP1 also interact in the absence of Ca²⁺, thus independent of S100P. Direct ezrin-IQGAP1 interaction can be shown with the purified proteins. It is mediated via the N-terminal FERM domain of ezrin and the IQ domain of IQGAP1, respectively. Ezrin and IQGAP1 colocalize in the submembraneous cytoskeleton and in cellular protrusions of human epithelial cells and knockdown of ezrin reduces the cortical localization of IQGAP1. Thus, ezrin appears to participate in recruiting IQGAP1 to the cell cortex thereby establishing a close connection between membrane-F-actin contacts and actin regulators that can be assembled by IQGAP1. This article is part of a Special Issue entitled: 13th European Symposium on Calcium.

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Heterodimeric interaction and interfaces of S100A1 and S100P

Cited by 32 publications

References 40 publications

Mutually antagonistic actions of S100A4 and S100A1 on normal and metastatic phenotypes

Mutually antagonistic actions of S100A4 and S100A1 on normal and metastatic phenotypes

Ca2+ signaling in mouse cardiomyocytes with ablated S100A1 protein

Ezrin interacts with the scaffold protein IQGAP1 and affects its cortical localization

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