scholarly journals WISp39 binds phosphorylated Coronin 1B to regulate Arp2/3 localization and Cofilin-dependent motility

2015 ◽  
Vol 208 (7) ◽  
pp. 961-974 ◽  
Author(s):  
Michael Howell ◽  
Howard Brickner ◽  
Violaine D. Delorme-Walker ◽  
Justin Choi ◽  
Jean-Michel Saffin ◽  
...  
Keyword(s):  
Cell Migration ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Mammalian Cells ◽  
Morphological Changes ◽  
Leading Edge ◽  
Heat Shock Protein 90 ◽  
Binding Partner ◽  
Directed Cell Migration ◽  
Essential Function

We previously identified Waf1 Cip1 stabilizing protein 39 (WISp39) as a binding partner for heat shock protein 90 (Hsp90). We now report that WISp39 has an essential function in the control of directed cell migration, which requires WISp39 interaction with Hsp90. WISp39 knockdown (KD) resulted in the loss of directional motility of mammalian cells and profound changes in cell morphology, including the loss of a single leading edge. WISp39 binds Coronin 1B, known to regulate the Arp2/3 complex and Cofilin at the leading edge. WISp39 preferentially interacts with phosphorylated Coronin 1B, allowing it to complex with Slingshot phosphatase (SSH) to dephosphorylate and activate Cofilin. WISp39 also regulates Arp2/3 complex localization at the leading edge. WISp39 KD-induced morphological changes could be rescued by overexpression of Coronin 1B together with a constitutively active Cofilin mutant. We conclude that WISp39 associates with Hsp90, Coronin 1B, and SSH to regulate Cofilin activation and Arp2/3 complex localization at the leading edge.

scholarly journals RNA-binding proteins and heat-shock protein 90 are constituents of the cytoplasmic capping enzyme interactome

2018 ◽  
Vol 293 (43) ◽  
pp. 16596-16607 ◽  
Author(s):  
Jackson B. Trotman ◽  
Bernice A. Agana ◽  
Andrew J. Giltmier ◽  
Vicki H. Wysocki ◽  
Daniel R. Schoenberg
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Mammalian Cells ◽  
Binding Proteins ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Heat Shock Protein 90 ◽  
Hsp90 Inhibitor ◽  
Capping Enzyme ◽  
Eukaryotic Mrnas

The N7-methylguanosine cap is added in the nucleus early in gene transcription and is a defining feature of eukaryotic mRNAs. Mammalian cells also possess cytoplasmic machinery for restoring the cap at uncapped or partially degraded RNA 5′ ends. Central to both pathways is capping enzyme (CE) (RNA guanylyltransferase and 5′-phosphatase (RNGTT)), a bifunctional, nuclear and cytoplasmic enzyme. CE is recruited to the cytoplasmic capping complex by binding of a C-terminal proline-rich sequence to the third Src homology 3 (SH3) domain of NCK adapter protein 1 (NCK1). To gain broader insight into the cellular context of cytoplasmic recapping, here we identified the protein interactome of cytoplasmic CE in human U2OS cells through two complementary approaches: chemical cross-linking and recovery with cytoplasmic CE and protein screening with proximity-dependent biotin identification (BioID). This strategy unexpectedly identified 66 proteins, 52 of which are RNA-binding proteins. We found that CE interacts with several of these proteins independently of RNA, mediated by sequences within its N-terminal triphosphatase domain, and we present a model describing how CE-binding proteins may function in defining recapping targets. This analysis also revealed that CE is a client protein of heat shock protein 90 (HSP90). Nuclear and cytoplasmic CEs were exquisitely sensitive to inhibition of HSP90, with both forms declining significantly following treatment with each of several HSP90 inhibitors. Importantly, steady-state levels of capped mRNAs decreased in cells treated with the HSP90 inhibitor geldanamycin, raising the possibility that the cytotoxic effect of these drugs may partially be due to a general reduction in translatable mRNAs.

Lipopolysaccharide pretreatment promotes cardiac stem cell migration through heat shock protein 90-dependent β-catenin activation

Life Sciences ◽  
2016 ◽  
Vol 153 ◽  
pp. 132-140 ◽  
Author(s):  
Li Zhang ◽  
Wei-Ran Geng ◽  
Jue Hu ◽  
Xiao-Ming Chen ◽  
Yue-Liang Shen ◽  
...  
Keyword(s):  
Stem Cell ◽  
Cell Migration ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Cardiac Stem Cell ◽  
Stem Cell Migration

scholarly journals Heat Shock Protein 27 Phosphorylation Regulates Tumor Cell Migration under Shear Stress

Biomolecules ◽  
2019 ◽  
Vol 9 (2) ◽  
pp. 50 ◽  
Author(s):  
Baohong Zhang ◽  
Fei Xie ◽  
Aziz Aziz ◽  
Shuai Shao ◽  
Wang Li ◽  
...  
Keyword(s):  
Shear Stress ◽  
Cell Migration ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Tumor Cell ◽  
Fluorescent Protein ◽  
Resonance Energy ◽  
Leading Edge ◽  
Heat Shock Protein 27 ◽  
Tumor Cell Migration

Heat shock protein 27 (HSP27) is a multifunctional protein that undergoes significant changes in its expression and phosphorylation in response to shear stress stimuli, suggesting that it may be involved in mechanotransduction. However, the mechanism of HSP27 affecting tumor cell migration under shear stress is still not clear. In this study, HSP27-enhanced cyan fluorescent protein (ECFP) and HSP27-Ypet plasmids are constructed to visualize the self-polymerization of HSP27 in living cells based on fluorescence resonance energy transfer technology. The results show that shear stress induces polar distribution of HSP27 to regulate the dynamic structure at the cell leading edge. Shear stress also promotes HSP27 depolymerization to small molecules and then regulates polar actin accumulation and focal adhesion kinase (FAK) polar activation, which further promotes tumor cell migration. This study suggests that HSP27 plays an important role in the regulation of shear stress-induced HeLa cell migration, and it also provides a theoretical basis for HSP27 as a potential drug target for metastasis.

scholarly journals Activation of Gαi3 triggers cell migration via regulation of GIV

2008 ◽  
Vol 182 (2) ◽  
pp. 381-393 ◽  
Author(s):  
Pradipta Ghosh ◽  
Mikel Garcia-Marcos ◽  
Scott J. Bornheimer ◽  
Marilyn G. Farquhar
Keyword(s):  
Signal Transduction ◽  
Wound Healing ◽  
Cell Migration ◽  
Mammalian Cells ◽  
Leading Edge ◽  
Akt Signaling ◽  
Actin Remodeling ◽  
Tumor Cell Migration ◽  
Binding Partner ◽  
Macrophage Chemotaxis

During migration, cells must couple direction sensing to signal transduction and actin remodeling. We previously identified GIV/Girdin as a Gαi3 binding partner. We demonstrate that in mammalian cells Gαi3 controls the functions of GIV during cell migration. We find that Gαi3 preferentially localizes to the leading edge and that cells lacking Gαi3 fail to polarize or migrate. A conformational change induced by association of GIV with Gαi3 promotes Akt-mediated phosphorylation of GIV, resulting in its redistribution to the plasma membrane. Activation of Gαi3 serves as a molecular switch that triggers dissociation of Gβγ and GIV from the Gi3–GIV complex, thereby promoting cell migration by enhancing Akt signaling and actin remodeling. Gαi3–GIV coupling is essential for cell migration during wound healing, macrophage chemotaxis, and tumor cell migration, indicating that the Gαi3–GIV switch serves to link direction sensing from different families of chemotactic receptors to formation of the leading edge during cell migration.

Heat Shock Protein 90 Inhibitor (17-AAG) Induces Apoptosis and Decreases Cell Migration/Motility of Keloid Fibroblasts

2015 ◽  
Vol 136 (1) ◽  
pp. 44e-53e ◽  
Author(s):  
In Sik Yun ◽  
Mi Hee Lee ◽  
Dong Kyun Rah ◽  
Dae Hyun Lew ◽  
Jong-Chul Park ◽  
...  
Keyword(s):  
Cell Migration ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Keloid Fibroblasts
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