Translocation and Phosphorylation of Calcyclin Binding Protein during Retinoic Acid-induced Neuronal Differentiation of Neuroblastoma SH-SY5Y Cells

Wu, Jing; Tan, Xin; Pan, Xiao; Yuan, Jing; Qiang, Bo

doi:10.5483/bmbrep.2003.36.4.354

Cited by 31 publications

(28 citation statements)

References 16 publications

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“…Results from others (Filipek et al, 2002b;Wu et al, 2003) and our studies suggest that phosphorylation and nuclear translocation are crucial for the function of SIP. We further demonstrate that phosphorylation at the Ser141 residue, the N-terminal region (aa 1-43) and the putative NLS region (aa 143-159) are crucial for nuclear translocation of SIP.…”

Section: Discussionsupporting

confidence: 68%

“…These data suggest that other modifications, besides the total amount of SIP protein, also contribute to the intensity change of SIP spot on 2D gel. It has been demonstrated that SIP is phosphorylated in unknown serine residues in neuroblastoma cells upon KCl or retinoic acid treatment (Filipek et al, 2002b;Wu et al, 2003). Furthermore, phosphorylation may cause changes in both isoelectric point and molecular weight of protein and therefore lead to the relocation of protein spots on 2D gel.…”

Section: Resultsmentioning

confidence: 99%

“…We next examined whether the cellular localization of SIP changed upon curcumin treatment, considering that it underwent both nuclear translocation and phosphorylation in KCl-or retinoic acid-treated cells (Filipek et al, 2002b;Wu et al, 2003). Using immunofluorescence staining, we found that curcumin exposure caused a significant translocation of endogenous SIP from the cytoplasm to nucleus in both MOLT-4 and MOLT-4/TG but not in MOLT-4/AraG cells ( Figure 3a).…”

Section: Resultsmentioning

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: Discussionsupporting

confidence: 68%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

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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“…This phenomenon has also been observed in retinoic acid-induced neuronal differentiation of neuroblastoma SH-SY5Y cells (Wu et al 2003). However, the significance of CacyBP/ SIP nuclear translation was unknown.…”

mentioning

confidence: 78%

Expression of Calcyclin-binding Protein/Siah-1 Interacting Protein in Normal and Malignant Human Tissues: An Immunohistochemical Survey

Zhai

Shi

Jin

et al. 2008

J Histochem Cytochem.

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(LD) S U M M A R Y Calcyclin-binding protein (CacyBP)/Siah-1 interacting protein (SIP), a component of ubiquitin-mediated proteolysis, could bind the Skp1-Cul1-F box protein complex. Although CacyBP/SIP was implicated in p53-induced b-catenin degradation, its exact function was still unknown. Our previous studies showed that CacyBP/SIP could modulate the multidrug-resistant phenotype of gastric cancer cells and was highly expressed in gastric cancer tissues compared with that in non-cancerous tissues. In this study, CacyBP/SIP protein expression profile in a broad range of human normal tissues and carcinomas was analyzed by immunohistochemistry staining with anti-CacyBP/SIP monoclonal antibody first produced in our laboratory. CacyBP/SIP was generally localized in the cytoplasm/nucleus. Positive staining of CacyBP/SIP was found in brain, heart, lymph node, and esophagus. Weak staining was shown in the rectum and kidney. No CacyBP/SIP was detected in other normal tissues. However, CacyBP/SIP was ubiquitously detected in all kinds of tumor tissues and was highly expressed in nasopharyngeal carcinoma, osteogenic sarcoma, and pancreatic cancer. To our knowledge, this is the first study on the CacyBP/SIP expression pattern in a broad range of human normal and tumor tissues. The data presented should serve as a useful reference for other investigators in future studies of CacyBP/SIP functions. Hopefully, this knowledge will lead to discovery of more roles of CacyBP/SIP in tumorigenesis. (J Histochem Cytochem 56:765-772, 2008)

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“…Unlike the complex above, the actions of this ligase complex do not depend on the phosphorylation status of CTNNB1 (Filipek 2006). CACYBP does, however, show changes in cellular localization under different conditions, which might depend on its own serine phosphorylation status (Filipek et al 2002;Wu et al 2003). Two recent reviews (Filipek 2006;Fukushima et al 2006) summarize what is presently known about the role of CACYBP in an E3 ligase complex, and it is clear that more work is needed before we completely understand its role in CTNNB1 degradation and how it is controlled.…”

mentioning

confidence: 99%

β-Catenin (CTNNB1) in the Mouse Uterus During Decidualization and the Potential Role of Two Pathways in Regulating Its Degradation

Herington

Martin

et al. 2007

J Histochem Cytochem.

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S U M M A R Y b-catenin plays a role in cell adhesion and as a transcriptional coactivator. Its levels are regulated in cells by controlling its degradation through ubiquitination by two different E3 ligase complexes. One complex contains b-transducing repeat containing (BTRC) protein, which binds to b-catenin when phosphorylated on specific (S33 and S37) residues, whereas the other involves calcyclin-binding protein (CACYBP). The aim of this study was to determine the localization and levels of total and active (S33/S37-dephosphorylated) b-catenin in the pregnant mouse uteri and those undergoing artificially stimulated decidualization. These two forms of b-catenin were localized almost exclusively to the endometrial epithelia just prior to the onset of implantation. Although this localization continued after the onset of implantation, there were less epithelial cells present in areas of the uterus undergoing decidualization. Rather, there was a progressive increase in b-catenin localization in endometrial stromal cells undergoing decidualization in the anti-mesometrial and, to a lesser extent, in the mesometrial regions. The presence of a conceptus was not required for the changes in localization seen in the pregnant uterus because similar findings were also seen in uteri undergoing artificially stimulated decidualization. Finally, overall levels of total, active (S33 and S37 dephosphorylated), and phosphorylated (S33/S37/T42) b-catenin protein and the steady-state levels of calcyclin-binding protein mRNA changed in the uterus during decidualization. The result of this study shows the changing localization and levels of b-catenin in the mouse uterus during decidualization. Further, the results suggest potential roles for both the BTRC and CACYBP E3 ligase mechanisms of b-catenin ubiquitination in the uterus during decidualization. (J Histochem Cytochem 55:963-974, 2007)

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Translocation and Phosphorylation of Calcyclin Binding Protein during Retinoic Acid-induced Neuronal Differentiation of Neuroblastoma SH-SY5Y Cells

Cited by 31 publications

References 16 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

Expression of Calcyclin-binding Protein/Siah-1 Interacting Protein in Normal and Malignant Human Tissues: An Immunohistochemical Survey

β-Catenin (CTNNB1) in the Mouse Uterus During Decidualization and the Potential Role of Two Pathways in Regulating Its Degradation

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