Identification of Proteins Interacting with Dysferlin Using the Tandem Affinity Purification Method

Assadi, Maziar; Schindler, Thomas; Müller, Bernd; Porter, John D.; Rüegg, Markus A.; Langen, Hanno

doi:10.2174/1874085500801010017

Cited by 5 publications

(4 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…After we treated the samples with ComBat which reduced the aforementioned bias ( Fig. 3 a, b, c right) the correlation value increased to 0.62 which could indicate a possible functional association between DYSF and SYNPO2L [72].…”

Section: Improved Combined Data Quality After the Correction Of Batchmentioning

confidence: 95%

MyoMiner: explore gene co-expression in normal and pathological muscle

et al. 2020

View full text Add to dashboard Cite

Background: High-throughput transcriptomics measures mRNA levels for thousands of genes in a biological sample. Most gene expression studies aim to identify genes that are differentially expressed between different biological conditions, such as between healthy and diseased states. However, these data can also be used to identify genes that are co-expressed within a biological condition. Gene co-expression is used in a guilt-byassociation approach to prioritize candidate genes that could be involved in disease, and to gain insights into the functions of genes, protein relations, and signaling pathways. Most existing gene co-expression databases are generic, amalgamating data for a given organism regardless of tissue-type. Methods: To study muscle-specific gene co-expression in both normal and pathological states, publicly available gene expression data were acquired for 2376 mouse and 2228 human striated muscle samples, and separated into 142 categories based on species (human or mouse), tissue origin, age, gender, anatomic part, and experimental condition. Co-expression values were calculated for each category to create the MyoMiner database. Results: Within each category, users can select a gene of interest, and the MyoMiner web interface will return all correlated genes. For each co-expressed gene pair, adjusted p-value and confidence intervals are provided as measures of expression correlation strength. A standardized expression-level scatterplot is available for every gene pair r-value. MyoMiner has two extra functions: (a) a network interface for creating a 2-shell correlation network, based either on the most highly correlated genes or from a list of genes provided by the user with the option to include linked genes from the database and (b) a comparison tool from which the users can test whether any two correlation coefficients from different conditions are significantly different. Conclusions: These co-expression analyses will help investigators to delineate the tissue-, cell-, and pathologyspecific elements of muscle protein interactions, cell signaling and gene regulation. Changes in co-expression between pathologic and healthy tissue may suggest new disease mechanisms and help define novel therapeutic targets. Thus, MyoMiner is a powerful muscle-specific database for the discovery of genes that are associated with related functions based on their co-expression.

show abstract

Section: Improved Combined Data Quality After the Correction Of Batchmentioning

confidence: 95%

MyoMiner: explore gene co-expression in normal and pathological muscle

et al. 2020

View full text Add to dashboard Cite

show abstract

“…Muscle health and function are heavily tied to intracellular membrane trafficking, central to the related processes, dysferlin’s interaction with other key proteins involved in vesicle trafficking (see Section 3.2 ) [ 16 , 153 , 154 ]. The clinical manifestations of dysferlinopathy are also marked by increased inflammation, potentially exacerbating the disease’s progression [ 108 , 124 ].…”

Section: Dysferlin: a Mosaic Of Uncharted Roles And Functionalitiesmentioning

confidence: 99%

The Dysferlinopathies Conundrum: Clinical Spectra, Disease Mechanism and Genetic Approaches for Treatments

Anwar,

Yokota

2024

Biomolecules

View full text Add to dashboard Cite

Dysferlinopathies refer to a spectrum of muscular dystrophies that cause progressive muscle weakness and degeneration. They are caused by mutations in the DYSF gene, which encodes the dysferlin protein that is crucial for repairing muscle membranes. This review delves into the clinical spectra of dysferlinopathies, their molecular mechanisms, and the spectrum of emerging therapeutic strategies. We examine the phenotypic heterogeneity of dysferlinopathies, highlighting the incomplete understanding of genotype-phenotype correlations and discussing the implications of various DYSF mutations. In addition, we explore the potential of symptomatic, pharmacological, molecular, and genetic therapies in mitigating the disease’s progression. We also consider the roles of diet and metabolism in managing dysferlinopathies, as well as the impact of clinical trials on treatment paradigms. Furthermore, we examine the utility of animal models in elucidating disease mechanisms. By culminating the complexities inherent in dysferlinopathies, this write up emphasizes the need for multidisciplinary approaches, precision medicine, and extensive collaboration in research and clinical trial design to advance our understanding and treatment of these challenging disorders.

show abstract

“…Since dysferlin contains a transmembrane domain anchored to phospholipids in both vesicle and plasma membranes, it is thought to co-ordinate vesicle docking and fusion with help from cytosolic protein-binding partners that do not contain membrane-spanning regions such as S100A10, Annexin A2 (ANX2), AHNAK, and TRIM72 (MG53) [ 82 , 145 , 146 ]. Supporting this, multiple large-scale proteomics experiments have identified interactions between dysferlin and over 100 other proteins, including many implicated in membrane repair [ 145 , 147 , 148 ]. Fluorescence-imaging experiments using mouse myoblasts show possible associations between dysferlin, TRIM72, and caveolin-3 (Cav3) that facilitates intracellular vesicle trafficking during acute damage membrane repair [ 82 ].…”

Section: Different Roles For Ca 2+ Sensor Proteins...mentioning

confidence: 99%

Role of calcium-sensor proteins in cell membrane repair

Shaw

2023

Bioscience Reports

View full text Add to dashboard Cite

Cell membrane repair is a critical process used to maintain cell integrity and survival from potentially lethal chemical, and mechanical membrane injury. Rapid increases in local calcium levels due to a membrane rupture have been widely accepted as a trigger for multiple membrane resealing models that utilize exocytosis, endocytosis, patching and shedding mechanisms. Calcium sensor proteins, such as synaptotagmins, dysferlin, S100 proteins and annexins have all been identified to regulate, or participate in, multiple modes of membrane repair. Dysfunction of membrane repair from inefficiencies or genetic alterations in these proteins contributes to diseases such as muscular dystrophy and heart disease. This review covers the role of some of the key calcium sensor proteins and their involvement in membrane repair.

show abstract

Identification of Proteins Interacting with Dysferlin Using the Tandem Affinity Purification Method

Cited by 5 publications

References 25 publications

MyoMiner: explore gene co-expression in normal and pathological muscle

MyoMiner: explore gene co-expression in normal and pathological muscle

The Dysferlinopathies Conundrum: Clinical Spectra, Disease Mechanism and Genetic Approaches for Treatments

Role of calcium-sensor proteins in cell membrane repair

Contact Info

Product

Resources

About