𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Tyrosine phosphorylation controls nuclear localization and transcriptional activity of Ssdp1 in mammalian cells

✍ Scribed by Ipsita Dey-Guha; Nasir Malik; Renaud Lesourne; Paul E. Love; Heiner Westphal

Publisher
John Wiley and Sons
Year
2008
Tongue
English
Weight
393 KB
Volume
103
Category
Article
ISSN
0730-2312

No coin nor oath required. For personal study only.

✦ Synopsis

Abstract

The LIM‐HD proteins interact with different cofactors, including Ssdp1 to regulate development in a diverse range of species. The single stranded DNA binding protein (Ssdp1) is a member of an evolutionarily conserved family of proteins that regulate critical transcriptional processes during embryonic development. Ssdp1 is localized predominantly in the cytoplasm of 293T cells but is translocated to the nucleus when co‐transfected with Lck, a member of the Src family of non‐receptor tyrosine kinases. The Src tyrosine kinase inhibitor PP2 blocked the nuclear translocation of Ssdp1. Western blot analysis showed that co‐expression of Ssdp1 and Lck in 293T cells induces Ssdp1 phosphorylation. Mutation of the Ssdp1 N terminal tyrosine residues 23 and 25 markedly reduced both the phosphorylation and the nuclear localization of Ssdp1. Lck enhanced the transcriptional activity of Ssdp1 in the context of known components of a LIM‐homeodomain (LIM‐HD)/cofactor complex. We propose that phosphorylation involving N‐terminal tyrosine residues of Ssdp1 is a means of regulating its nuclear localization and subsequent transcriptional activation of LIM‐HD complexes. J. Cell. Biochem. 103: 1856–1865, 2007. © 2007 Wiley‐Liss, Inc.

📜 SIMILAR VOLUMES

Tyrosine phosphorylation/dephosphorylati
Tyrosine phosphorylation/dephosphorylation controls capping of Fc? receptor II in U937 cells
✍ Kwiatkowska, Katarzyna ;Sobota, Andrzej 📂 Article 📅 1999 🏛 John Wiley and Sons 🌐 English ⚖ 262 KB

In the capping of cell-surface receptors two stages can be distinguished: 1) clustering of the receptors (patching) induced by cross-linking with specific antibodies and 2) subsequent assembly of patches into a cap which is driven by the actin-based cytoskeleton. We found that patching of Fc␥ recept

Nuclear localization and DNA interaction
Nuclear localization and DNA interaction of protein disulfide isomerase ERp57 in mammalian cells
✍ Sabina Coppari; Fabio Altieri; Anna Ferraro; Silvia Chichiarelli; Margherita Euf 📂 Article 📅 2002 🏛 John Wiley and Sons 🌐 English ⚖ 203 KB

## Abstract Protein disulfide isomerase ERp57 is localized predominantly in the endoplasmic reticulum, but is also present in the cytosol and, according to preliminary evidence, in the nucleus of avian cells. Conclusive evidence of its nuclear localization and of its interaction with DNA in vivo in

Resistance to 1,25D-induced differentiat
Resistance to 1,25D-induced differentiation in human acute myeloid leukemia HL60-40AF cells is associated with reduced transcriptional activity and nuclear localization of the vitamin D receptor
✍ Edward Garay; Robert Donnelly; Xuening Wang; George P. Studzinski 📂 Article 📅 2007 🏛 John Wiley and Sons 🌐 English ⚖ 438 KB

## Abstract The anti‐neoplastic effects of 1,25‐dihydroxyvitamin D~3~ (1,25D) are well documented in numerous tumor cell systems and animal models of cancer. However, despite this pre‐clinical success, the clinical use of 1,25D is currently impeded by the dose‐limiting hypercalcemia, and the risk o

Correlation of constitutive activation o
Correlation of constitutive activation of raf-1 with morphological transformation and abrogation of tyrosine phosphorylation of distinct sets of proteins in human squamous carcinoma cells
✍ Bharvin K. R. Patel; Sugata Ray; Theresa L. Whiteside; Usha Kasid 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 162 KB 👁 1 views

We and others have reported an association between raf-1 protein serine/threonine kinase activity and transformation of mammalian cells. Because constitutive tyrosine phosphorylation of specific polypeptides is, in general, indicative of the transformed state of cells, we investigated the effect of

Adhesion of HT-29 colon carcinoma cells
Adhesion of HT-29 colon carcinoma cells to E-selectin results in increased tyrosine phosphorylation and decreased activity of c-src
✍ Sharon A. Soltesz; Elaine A. Powers; Jian-Guo Geng; Chris Fisher 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 French ⚖ 266 KB

Adhesion of metastatic cancer cells at secondary sites is known to be regulated by several families of adhesion proteins, including selectins and integrins. Colon carcinoma cells have been shown to tether to and roll on both stimulated endothelial cells and purified E-selectin. We have demonstrated