Phosphorylation Modulates the Subcellular Localization of SOX11

Balta, Elli-Anna; Wittmann, Marie-Theres; Jung, Matthias; Sock, Elisabeth; Haeberle, Benjamin Martin; Heim, Birgit; Zweydorf, Felix von; Heppt, Jana; Wittgenstein, Julia von; Gloeckner, Christian Johannes; Lie, Dieter Chichung

doi:10.3389/fnmol.2018.00211

Cited by 24 publications

(19 citation statements)

References 48 publications

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“…To further investigate the mechanism of action of the cholinergic pathway in SCI, we determined the expression of Chrm2 and Chrnb2 in neurogenesis and their subcellular localization. Doublecortin (DCX) antibodies can be used to specifically label new neurons [12]. Under CNS injury state, DCX promotes the differentiation and maturation of new neural stem cells as well as promotes their migration from the origin to the lesion or damaged area to replace neurons.…”

Section: Resultsmentioning

confidence: 99%

Transcriptomic analysis of α-synuclein knockdown after T3 spinal cord injury in rats

Zeng

Liu

et al. 2019

BMC Genomics

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Background: Endogenous α-synuclein (α-Syn) is involved in many pathophysiological processes in the secondary injury stage after acute spinal cord injury (SCI), and the mechanism governing these functions has not been thoroughly elucidated to date. This research aims to characterize the effect of α-Syn knockdown on transcriptional levels after SCI and to determine the mechanisms underlying α-Syn activity based on RNA-seq. Result: The establishment of a rat model of lentiviral vector-mediated knockdown of α-Syn in Sprague-Dawley rats with T3 spinal cord contusion (LV_SCI group). The results of the RNA-seq analysis showed that there were 337 differentially expressed genes (DEGs) between the SCI group and the LV_SCI group, and 153 DEGs specific to LV_ SCI between the (SCI vs LV_SCI) and (SCI vs CON) comparisons. The top 20 biological transition terms were identified by Gene ontology (GO) analysis. The Kyoto Gene and Genomic Encyclopedia (KEGG) analysis showed that the LV_SCI group significantly upregulated the cholinergic synaptic & nicotine addiction and the neuroactive ligand receptor interaction signaling pathway. Enriched chord analysis analyzes key genes. Further cluster analysis, gene and protein interaction network analysis and RT-qPCR results showed that Chrm2 and Chrnb2 together significantly in both pathways. The proliferation of muscarinic cholinergic receptor subtype 2 (Chrm2) and nicotinic cholinergic receptor subtype β2 (Chrnb2), and the neurogenesis were elevated in the injury site of LV_SCI group by immunofluorescence. Further by subcellular localization, the LV_SCI group enhanced the expression of Chrnb2 at the cell membrane. Conclusion: Knockdown of α-Syn after SCI enhance motor function and promote neurogenesis probably through enhancing cholinergic signaling pathways and neuroreceptor interactions. This study not only further clarifies the understanding of the mechanism of knockdown of α-Syn on SCI but also helps to guide the treatment strategy for SCI.

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Section: Resultsmentioning

confidence: 99%

Transcriptomic analysis of α-synuclein knockdown after T3 spinal cord injury in rats

Zeng

Liu

et al. 2019

BMC Genomics

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“…The subcellular localisation of SOX11 can be informative for cancer classification since high SOX11 mRNA levels and detection of the nuclear protein are reliable markers of mantle cell lymphoma ( Mozos et al, 2009 ). During neurogenesis, SOX11 is detected in both the nucleus and cytoplasm ( Balta et al, 2018 ). Phosphorylation of specific serine residues can modulate SOX11 subcellular localisation and prevent its nuclear localisation ( Balta et al, 2018 ).…”

Section: Discussionmentioning

confidence: 99%

“…During neurogenesis, SOX11 is detected in both the nucleus and cytoplasm ( Balta et al, 2018 ). Phosphorylation of specific serine residues can modulate SOX11 subcellular localisation and prevent its nuclear localisation ( Balta et al, 2018 ). We have not determined whether SOX11 localises to the cytoplasm, as well as the nucleus, in breast cancer case samples, and if SOX11 localisation could be useful for classification of breast cancers.…”

Section: Discussionmentioning

confidence: 99%

SOX11 promotes epithelial/mesenchymal hybrid state and alters tropism of invasive breast cancer cells

Oliemuller

Newman

Tsang

et al. 2020

eLife

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SOX11 is an embryonic mammary epithelial marker that is normally silenced prior to birth. High SOX11 levels in breast tumours are significantly associated with distant metastasis and poor outcome in breast cancer patients. Here, we show that SOX11 confers distinct features to ER-negative DCIS.com breast cancer cells, leading to populations enriched with highly plastic hybrid epithelial/mesenchymal cells, which display invasive features and alterations in metastatic tropism when xenografted into mice. We found that SOX11+DCIS tumour cells metastasize to brain and bone at greater frequency and to lungs at lower frequency compared to cells with lower SOX11 levels. High levels of SOX11 leads to the expression of markers associated with mesenchymal state and embryonic cellular phenotypes. Our results suggest that SOX11 may be a potential biomarker for breast tumours with elevated risk of developing metastases and may require more aggressive therapies.

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“…One of the biological outcomes of protein phosphorylation is its influence on the interplay with other molecules such as proteins, nucleic acids, or cofactors. Consequently, a modified protein may gain new biological properties and change its cellular behavior, manifested as different intracellular dynamics or subcellular localization [60,61]. Thus, in line with this idea, we tested the biological relevance of all PTMs within four determined residues, Y24/T59 and S304/ S307 at the N and C termini, respectively.…”

Section: Discussionmentioning

confidence: 99%

Phosphorylation of the N‐terminal domain of ribosomal P‐stalk protein uL10 governs its association with the ribosome

et al. 2020

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The uL10 protein is the main constituent of the ribosomal P‐stalk, anchoring the whole stalk to the ribosome through interactions with rRNA. The P‐stalk is the core of the GTPase‐associated center (GAC), a critical element for ribosome biogenesis and ribosome translational activity. All P‐stalk proteins (uL10, P1, and P2) undergo phosphorylation within their C termini. Here, we show that uL10 has multiple phosphorylation sites, mapped also within the N‐terminal rRNA‐binding domain. Our results reveal that the introduction of a negative charge within the N terminus of uL10 impairs its association with the ribosome. These findings demonstrate that uL10 N‐terminal phosphorylation has regulatory potential governing the uL10 interaction with the ribosome and may control the activity of GAC.

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Phosphorylation Modulates the Subcellular Localization of SOX11

Cited by 24 publications

References 48 publications

Transcriptomic analysis of α-synuclein knockdown after T3 spinal cord injury in rats

Transcriptomic analysis of α-synuclein knockdown after T3 spinal cord injury in rats

SOX11 promotes epithelial/mesenchymal hybrid state and alters tropism of invasive breast cancer cells

Phosphorylation of the N‐terminal domain of ribosomal P‐stalk protein uL10 governs its association with the ribosome

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