Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The role of Tau regulating MSI1 interactome

ABSTRACT: This project is to identify the MSI protein interaction networks and the role of Tau in regulating MSI1 protein interaction netowrk

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell

SUBMITTER: Yingxin Zhao

LAB HEAD: Yingxin Zhao

PROVIDER: PXD049253 | Pride | 2026-04-06

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	MIS1-IP-A1-1.raw	Raw
	MIS1-IP-A1-2.raw	Raw
	MIS1-IP-A1-3.raw	Raw
	MIS1-IP-A3-1.raw	Raw
	MIS1-IP-A3-2.raw	Raw

Items per page:

1 - 5 of 26

Publications

Pathogenic oligomeric Tau alters neuronal RNA processes through the formation of nuclear heteromeric amyloids with RNA-binding protein Musashi1.

Puangmalai Nicha N Aday Abbigael E AE Samples Madison M Bhatt Nemil N Cascio Filippa Lo FL Marcatti Michela M Park Suhyeorn J SJ Fung Leiana L Jerez Cynthia C Penalva Luiz O LO Zhao Yingxin Y Hao Haiping H Lugano Doreen D Kayed Rakez R Montalbano Mauro M

Progress in neurobiology 20250308

Alzheimer's disease (AD) is marked by cytoplasmic proteinopathies, primarily involving misfolded Tau protein. Pathogenic Tau species, such as soluble oligomers and fibrils, disrupt RNA metabolism, though the mechanisms are unclear. Recent research indicates that RNA has a crucial role in Tau aggregation. Our study builds on this by noting significant co-deposition of RNA-Binding Proteins (RBPs) with Tau in AD and Frontotemporal dementia (FTLD) brains. Using molecular and cellular techniques, we ...[more]

PMID: 40064283

Similar Datasets

The Msi Family of RNA-Binding Proteins Function Redundantly as Intestinal Oncoproteins

Project description:Members of the Msi family of RNA-binding proteins have recently emerged as potent oncoproteins in a range of malignancies. MSI2 is highly expressed in hematopoietic cancers, where it is required for disease maintenance. In contrast to the hematopoietic system, colorectal cancers can express both Msi family members, MSI1 and MSI2. Here, we demonstrate that, in the intestinal epithelium, Msi1 and Msi2 have analogous oncogenic effects. Further, comparison of Msi1/2-induced gene expression programs and transcriptome-wide analyses of Msi1/2-RNA-binding targets reveal significant functional overlap, including induction of the PDK-Akt-mTORC1 axis. Ultimately, we demonstrate that concomitant loss of function of both MSI family members is sufficient to abrogate the growth of human colorectal cancer cells, and Msi gene deletion inhibits tumorigenesis in several mouse models of intestinal cancer. Our findings demonstrate that MSI1 and MSI2 act as functionally redundant oncoproteins required for the ontogeny of intestinal cancers.

2015-10-22 | GSE54598 | GEO

Cancer-specific association between Tau (MAPT) and cellular pathways, clinical outcome, and drug response

Project description:Tau (MAPT) is a microtubule-associated protein causing frequent neurodegenerative diseases or inherited frontotemporal lobar degenerations. Emerging evidence for non-canonical functions of Tau in DNA protection and P53 regulation suggests its involvement in cancer. Indeed, Tau expression correlates with cancer-specific survival or response to microtubule therapeutics. These data may imply common molecular pathways involved in the pathogenesis of neurodegenerative disorders and cancer. To bring new evidence that Tau represents a key protein in cancer, we present an in silico pan-cancer analysis of MAPT transcriptomic profile in over 11000 clinical samples and over 1300 pre-clinical samples provided by the TCGA and the DEPMAP datasets respectively. We completed this analysis by exploring a possible interplay of MAPT with wild-type or mutated P53. Then, we calculated the impact of MAPT expression on clinical outcome and drug response. Overall, the results support a relevant role of the MAPT gene in several cancer types, although the contribution of Tau to cancer appears to very much depend on the cellular context.

2022-11-27 | E-MTAB-8166 | biostudies-arrayexpress

Musashi proteins are post-transcriptional regulators of the epithelial-luminal cell state

Project description:mRNA-seq and ribosome profiling of neural stem cells overexpressing or knocked out for Musashi RNA-binding proteins Study of the global effects of Musashi (Msi) proteins on the transcriptome of embryonic neural stem cells. Neural stem cells were derived from brains of E12.5 or E13.5 embryos engineered to have inducible Msi1 or Msi2 genes, or from embryos with double floxed alleles of Msi1 and Msi2 carrying a Tamoxifen-induclble Cre (CreER). The overexpression mice were made using the Flp-in system (OpenBioSystems), where a cDNA of interest (in this case Msi1 or Msi2) is knocked into the Collagen (Col1A1) locus. The expression of the cDNA of interest is driven by m2rTTA that is knocked into the Rosa26 locus (R26). KH2 describes a strain containing the R26-m2rTTA but lacking Msi1 or Msi2 cDNA. MSI1 describes a strain containing R26-m2rTTA and Msi1 cDNA in Col1A1. MSI2 describes a strain containing R26-m2rTTA and Msi2 cDNA in Col1A1. C1 describes a strain lacking the CreER allele but containing double floxed alleles of Msi1/Msi2 (used as Tamoxifen control). C4 describes a strain carrying the CreER allele and double floxed alleles of Msi1/Msi2.

2014-06-13 | E-GEOD-58423 | biostudies-arrayexpress

Tau posttranslational modifications

Project description:Human tauopathies including Alzheimer's disease are characterized by alterations in the post-translational modification (PTM) pattern of Tau, leading to the formation of insoluble aggregates, neuronal dysfunction and degeneration. We immunoprecipitated Tau from post-mortem brain tissue of early stage Alzheimer's disease patients and age-matched controls, and analyzed PTMs on this soluble pool of Tau protein. In addition to known serine, threonine and tyrosine phosphorylation events, we identified a number of previously unknown monomethylation events on lysines in both control and Alzheimer's patient tissues.

2021-09-09 | PXD017065 | Pride

Msi1 integrates APC loss and mTORC1 activation to promote intestinal stem cell transformation

Project description:Loss of the APC tumor suppressor in the intestinal epithelium initiates the majority of human colorectal adenocarcinomas. Constitutive Î²-catenin activation is thought to underlie tumorigenesis induced by loss of APC, however Î²-catenin activation alone does not recapitulate all APC-loss phenotypes, suggesting that additional pathways are required. We demonstrate that aberrant activation of the Msi1 RNA binding protein occurs upon APC loss and that constitutive Msi1 activation alone is sufficient to phenocopy APC loss in the intestinal epithelium. Msi1 elicits these effects through binding of mRNAs encoding pleiotropic tumor suppressors resulting in promiscuous activation of quiescent intestinal stem cells, proliferative expansion of the stem cell compartment, crypt fission, and blocked differentiation. Further, we find these phenotypes to be largely dependent on mTORC1 activity, and demonstrate that loss of Msi activity is sufficient to abrogate tumorigenesis in mouse and human systems. Our findings implicate Msi1 as a central coordinator of APC loss-induced intestinal stem cell transformation and adenocarcinoma progression. 2 wild-type, 2 transgenic samples

2015-10-22 | E-GEOD-54598 | biostudies-arrayexpress

comparative proteomics of non-small cell lung cancer and small cell lung cancer

Project description:We aimed to identify the differences between these two subtypes of lung cancers and their differentially clinical treatment. Through functional analysis, we obtained differentially expressed proteins which might be assossciated with lung cancer treatment.

2019-09-25 | PXD015270 | Pride

PRR of Tau Crosslinking with Tubulin

Project description:We used cross-linking mass spectrometry with the cleavable cross-linker, disuccinimidyl dibutyric urea (DSBU) to map sites of interaction between the proline rich domain (PRR, tau amino acids 149-244) and tubulin. For comparison, we also conducted these experiments with PRR constructs containing multiple phosphomimic mutations (from serine or threonine to glutamate) at tau amino acid positions 181, 217, 231 and 235.

2026-03-09 | PXD049384 | Pride

Properties of Alzheimer’s disease brain-derived tau aggregates define tau processing by human astrocytes

Project description:The templated misfolding of tau proteins accounts for tau pathology spread in Alzheimer’s disease (AD). Post-translational modifications, including phosphorylation at specific residues, are closely linked with tau seeding ability and clinical disease progression. This study investigates the role of astrocytes in tau spread, demonstrating that tau aggregates from post-mortem AD brain are internalized and processed by human astrocytes. Differences in tau internalization, clearance, and seeding were observed, potentially reflecting the molecular properties of tau. A direct relationship between tau handling by astrocytes and astrocyte responses was noted in transcriptomic data, highlighting dysregulated genes linked to pathological tau clearance pathways. To explore these differences, mass spectrometry was performed on both control and AD brain extracts, providing insights into the complex interplay between tau diversity and astrocyte responses in AD.

2025-05-07 | PXD056614 | Pride

Msi1 assists CPEB1-driven polyadenylation [CPEB1 & Msi1 RIP replicate]

Project description:The translational reactivation of maternal mRNAs encoding the drivers of vertebrate meiosis is accomplished mainly by cytoplasmic polyadenylation. The Cytoplasmic Polyadenylation Elements (CPEs) present in the 3’ UTR of these transcripts, together with their cognate CPE-binding proteins (CPEBs), define a combinatorial code that determines the timing and extent of translational activation upon meiosis resumption. In addition, the RNA-binding protein Musashi1 (Msi1) regulates the polyadenylation of CPE-containing mRNAs by an as yet undefined CPEB-dependent or -independent mechanism. Here we show that Msi1 alone does not support cytoplasmic polyadenylation, but its binding triggers the remodeling of RNA structure, thereby exposing adjacent CPEs and stimulating polyadenylation. Thus, Msi1 directs the preferential use of specific CPEs, which in turn affects the timing and extent of polyadenylation during meiotic progression. Genome-wide analysis of CPEB1- and Msi-associated mRNAs identified 491 common targets, thus revealing a new layer of CPE-mediated translational control.

2017-07-17 | GSE68095 | GEO

Msi1 assists CPEB1-driven polyadenylation [CPEB1 RIP]

2017-07-17 | GSE68098 | GEO