CacyBP/SIP, a Calcyclin and Siah-1-interacting Protein, Binds EF-hand Proteins of the S100 Family

Filipek, Anna; Jastrzębska, Beata; Nowotny, Marcin; Kuźnicki, Jacek

doi:10.1074/jbc.m203602200

Cited by 135 publications

(109 citation statements)

References 34 publications

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“…Nuclear translocation of SIP is regulated by different motifs As reported (Filipek et al, 2002a;Santelli et al, 2005), the N-terminal amino acids (aa) 1-47 of SIP comprise a self-dimerization domain, and the C-terminal contains binding motifs for SKP1 and S100 proteins (Figure 4a). To explore the mechanisms underlying nuclear translocation of SIP, the protein sequence of SIP was analyzed computationally.…”

Section: Resultsmentioning

confidence: 81%

“…It has been shown that S100 family members interact with the C-terminal region of SIP (Filipek et al, 2002a;Bhattacharya et al, 2005) and some of the members, such as S100A1, S100A2, S100A6 and S100B, are involved in apoptosis regulation, and many S100 proteins display cellular translocation in response to various stimuli (Hsieh et al, 2002;Orre et al, 2007;Joo et al, 2008). Besides, SIP has been found to interact with ERK1/2 and downregulate ERK activity (Kilanczyk et al, 2009).…”

Section: Discussionmentioning

confidence: 99%

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Identification of Siah-interacting protein as a potential regulator of apoptosis and curcumin resistance

Luo

Yang

et al. 2010

Oncogene

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The mechanism underlying curcumin (diferuloylmethane) resistance is still largely unknown. Here we employed proteomic approach to identify the Siah-interacting protein (SIP) as a candidate for detailed study, because the spot intensity of SIP on a two-dimensional gel displayed 70-90% reduction in curcumin-sensitive cells, but remained unchanged in curcumin-resistant sublines, after curcumin treatment. Both gain-and loss-of-function studies revealed that SIP promoted curcumin-induced apoptosis. Moreover, SIP underwent phosphorylation and nuclear translocation in curcumin-sensitive but not resistant cells, upon curcumin exposure. The nuclear translocation of SIP was remarkably impaired when a putative nuclear localization sequence (NLS, amino acid (aa) 143-159) was deleted or the serine 141 was mutated into alanine, whereas truncation of the N-terminal region (aa 1-43) obviously increased the nuclear import of SIP. In accordance with their nuclear localization, N-terminal truncation significantly enhanced the proapoptotic effect of SIP, whereas NLS deletion or Ser141Ala mutation attenuated the apoptosis-promoting activity of both wildtype-and N-terminal truncated-SIP. These data suggest that SIP plays a role in apoptosis and curcumin resistance, and the function of SIP may be regulated by different motifs, such as the NLS, N-terminal region and serine 141. Our findings provide new insights into the biological significance of SIP and the mechanisms of drug resistance.

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Section: Resultsmentioning

confidence: 81%

Section: Discussionmentioning

confidence: 99%

Identification of Siah-interacting protein as a potential regulator of apoptosis and curcumin resistance

Luo

Yang

et al. 2010

Oncogene

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“…Previously, other members of S100A7 proteins such as S100A1, S100A6, S100A12, S100A7 inhibits SCCOC progression G Zhou et al S100B and S100P, were shown to interact with SIP in a calcium-dependent manner (Filipek et al, 2002). It remains to be determined whether S100A7 can also interact with SIP and participate in Siah-SIP-mediated b-catenin degradation as previously reported (Liu et al, 2001;Matsuzawa and Reed, 2001;Fukushima et al, 2006).…”

Section: Discussionmentioning

confidence: 81%

Reciprocal negative regulation between S100A7/psoriasin and β-catenin signaling plays an important role in tumor progression of squamous cell carcinoma of oral cavity

et al. 2008

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Overexpression of S100A7 (psoriasin), a small calciumbinding protein, has been associated with the development of psoriasis and carcinomas in different types of epithelia, but its precise functions are still unknown. Using human tissue specimens, cultured cell lines, and a mouse model, we found that S100A7 is highly expressed in preinvasive, well-differentiated and early staged human squamous cell carcinoma of the oral cavity (SCCOC), but little or no expression was found in poorly differentiated, later-staged invasive tumors. Interestingly, our results showed that S100A7 inhibits both SCCOC cell proliferation in vitro and tumor growth/invasion in vivo. Furthermore, we demonstrated that S100A7 is associated with the b-catenin complex, and inhibits b-catenin signaling by targeting b-catenin degradation via a noncanonical mechanism that is independent of GSK3b-mediated phosphorylation. More importantly, our results also indicated that b-catenin signaling negatively regulates S100A7 expression. Thus, this reciprocal negative regulation between S100A7 and b-catenin signaling implies their important roles in tumor development and progression. Despite its high levels of expression in early stage SCCOC tumorigenesis, S100A7 actually inhibits SCCOC tumor growth/invasion as well as tumor progression. Downregulation of S100A7 in later stages of tumorigenesis increases b-catenin signaling, leading to promotion of tumor growth and tumor progression.

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“…Calcyclin-binding protein (CacyBP), a 30 kDa protein, was identified on the basis of its ability to interact with S100 proteins, including S100A6, S100A1, S100A12, S100B, and S100P, in a calcium-dependent manner (1)(2)(3). CacyBP/SIP is highly expressed in the mouse and in rat brain, liver, spleen, and stomach, and weakly in rat lung and kidney (4).…”

Section: Introductionmentioning

confidence: 99%

Calcyclin-Binding Protein Inhibits Proliferation, Tumorigenicity, and Invasion of Gastric Cancer

Ning¹,

Sun

Li³

et al. 2007

Molecular Cancer Research

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Calcyclin-binding protein/Siah-1 -interacting protein (CacyBP/SIP), a target protein of the S100 family, which includes S100A6, S100A1, S100A12, S100B, and S100P, has been identified as a component of a novel ubiquitinylation complex leading to B-catenin degradation. However, the function of CacyBP/SIP in gastric cancer has not been elucidated. In the present study, we prepared CacyBP/SIP overexpressing and knockdown cell lines of gastric cancer. Forced CacyBP/SIP expression inhibited the proliferation of gastric cancer cells, suppressed tumorigenicity in vitro, and prolonged the survival time of tumor-bearing nude mice. In addition, increased CacyBP/SIP repressed the invasive potential of gastric cancer cells. Conversely, the down-regulation of CacyBP/SIP by RNA interference showed the opposite effects. Further studies showed that depressed CacyBP/SIP increased the expression of total and nuclear B-catenin at the protein level and elevated the transcriptional activity of Tcf/LEF. Taken together, our results suggest that CacyBP/SIP may be a potential inhibitor of cell growth and invasion in the gastric cancer cell, at least in part through the effect on B-catenin protein expression and transcriptional activation of Tcf/LEF.

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CacyBP/SIP, a Calcyclin and Siah-1-interacting Protein, Binds EF-hand Proteins of the S100 Family

Cited by 135 publications

References 34 publications

Identification of Siah-interacting protein as a potential regulator of apoptosis and curcumin resistance

Identification of Siah-interacting protein as a potential regulator of apoptosis and curcumin resistance

Reciprocal negative regulation between S100A7/psoriasin and β-catenin signaling plays an important role in tumor progression of squamous cell carcinoma of oral cavity

Calcyclin-Binding Protein Inhibits Proliferation, Tumorigenicity, and Invasion of Gastric Cancer

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