Phosphoproteomic Analysis Reveals Downstream PKA Effectors of AKAP Cypher/ZASP in the Pathogenesis of Dilated Cardiomyopathy

Lv, Jialan; Pan, Zhicheng; Chen, Jian; Xu, Rui; Wang, Dongfei; Huang, Jiaqi; Yang, Dong; Jiang, Jing; Yin, Xiaoxing; Cheng, Hongqiang; Guo, Xiaogang

doi:10.3389/fcvm.2021.753072

Cited by 3 publications

(2 citation statements)

References 60 publications

(93 reference statements)

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“…ZASP is a sarcomeric protein encoded by LDB3 and specifically expressed in human heart and skeletal muscle ( 16 ). It is well known that ZASP variants are associated with myopathies such as dilated cardiomyopathy (DCM) ( 17 ), left ventricular non-compaction cardiomyopathy (LVNC) ( 18 , 19 ), and HCM ( 20 ).…”

Section: Discussionmentioning

confidence: 99%

Case Report: Novel LIM domain-binding protein 3 (LDB3) mutations associated with hypertrophic cardiomyopathy family

Zheng

Huang²,

Hou³

et al. 2022

Front. Pediatr.

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Hypertrophic cardiomyopathy (HCM) is an autosomal dominant cardiomyopathy, which is one of the most common reasons for cardiac arrest in children or adolescents. It is characterized by ventricular hypertrophy (usually left ventricle), small ventricular cavity, and reduced ventricular diastolic compliance found by echocardiography in the absence of abnormal load (such as hypertension or aortic stenosis). HCM is usually caused by mutations in genes encoding sarcomere or sarcomere-related genes. Whole exome sequencing (WES) is performed to identify probable causative genes. Through WES, we identified LIM domain-binding protein 3 (LDB3) mutations (R547Q and P323S) respectively in an 11-year-old HCM girl and a 6-year-old HCM boy. Neural network analyses showed that the LDB3 (R547Q and P323S) mutation decreased its protein stability, with confidence scores of −0.9211 and −0.8967. The STRUM server also confirmed that the mutation decreased its protein stability. Thus, LDB3 mutation may be associated with heritable HCM. To our knowledge, this is the first time to report LDB3 heterozygous variants (R547Q and P323S) responsible for heritable HCM.

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Section: Discussionmentioning

confidence: 99%

Case Report: Novel LIM domain-binding protein 3 (LDB3) mutations associated with hypertrophic cardiomyopathy family

Zheng

Huang²,

Hou³

et al. 2022

Front. Pediatr.

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“…Moreover, α2β1 integrin can activate PDLIM1, but PDLIM1 may prevent α-actinin-1 from binding to integrin subunits and foci adhesion, directing the molecule to actin filaments and stress fibers [55]. ZASP can activate α5β1 integrins in mammals and αPS2βPS integrins in Drosophila with talin, and it can also activate integrins with vimentin [42,56]. PDLIM2 deficiency upregulates the expression of β1 integrin, leading to a loss of the normal phenotype in mammary epithelial cells [57].…”

Section: Integrin Signaling Pathwaymentioning

confidence: 99%

PDZ and LIM Domain-Encoding Genes: Their Role in Cancer Development

Jiang,

Xu,

Jiang

et al. 2023

Cancers

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PDZ-LIM family proteins (PDLIMs) are a kind of scaffolding proteins that contain PDZ and LIM interaction domains. As protein–protein interacting molecules, PDZ and LIM domains function as scaffolds to bind to a variety of proteins. The PDLIMs are composed of evolutionarily conserved proteins found throughout different species. They can participate in cell signal transduction by mediating the interaction of signal molecules. They are involved in many important physiological processes, such as cell differentiation, proliferation, migration, and the maintenance of cellular structural integrity. Studies have shown that dysregulation of the PDLIMs leads to tumor formation and development. In this paper, we review and integrate the current knowledge on PDLIMs. The structure and function of the PDZ and LIM structural domains and the role of the PDLIMs in tumor development are described.

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Using the Proteomics Toolbox to Resolve Topology and Dynamics of Compartmentalized cAMP Signaling

Kovanich

Low

Zaccolo

2023

IJMS

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cAMP is a second messenger that regulates a myriad of cellular functions in response to multiple extracellular stimuli. New developments in the field have provided exciting insights into how cAMP utilizes compartmentalization to ensure specificity when the message conveyed to the cell by an extracellular stimulus is translated into the appropriate functional outcome. cAMP compartmentalization relies on the formation of local signaling domains where the subset of cAMP signaling effectors, regulators and targets involved in a specific cellular response cluster together. These domains are dynamic in nature and underpin the exacting spatiotemporal regulation of cAMP signaling. In this review, we focus on how the proteomics toolbox can be utilized to identify the molecular components of these domains and to define the dynamic cellular cAMP signaling landscape. From a therapeutic perspective, compiling data on compartmentalized cAMP signaling in physiological and pathological conditions will help define the signaling events underlying disease and may reveal domain-specific targets for the development of precision medicine interventions.

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Phosphoproteomic Analysis Reveals Downstream PKA Effectors of AKAP Cypher/ZASP in the Pathogenesis of Dilated Cardiomyopathy

Cited by 3 publications

References 60 publications

Case Report: Novel LIM domain-binding protein 3 (LDB3) mutations associated with hypertrophic cardiomyopathy family

Case Report: Novel LIM domain-binding protein 3 (LDB3) mutations associated with hypertrophic cardiomyopathy family

PDZ and LIM Domain-Encoding Genes: Their Role in Cancer Development

Using the Proteomics Toolbox to Resolve Topology and Dynamics of Compartmentalized cAMP Signaling

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