A structural and functional dissection of the cardiac stress response factor MS1

Fogl, Claudia; Puckey, Loretto H.; Hinssen, Ulrike; Zaleska, Mariola; El-Mezgueldi, Mohammed; Croasdale, Rebecca; Bowman, Andrew; Matsukawa, Akihiro; Samani, Nilesh J.; Savva, Renos; Pfuhl, Mark

doi:10.1002/prot.23201

Cited by 10 publications

(16 citation statements)

References 38 publications

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“…Meanwhile, enrichment analysis revealed that ABRACL is mostly enriched in some signaling pathways, such as cell cycle, TNFR pathway, proteasome degradation, and mitochondrial pathway (Wang et al, 2019). Studies have found that ABRACL bears a similar structure to ABD2 and may be a transcriptional synergistic activator (Fogl et al, 2012, Galkin et al, 2008, Lin et al, 2011) that is closely related to cell cycle (Baumann et al, 2018). In this study, dual-luciferase reporter assay demonstrated that ABRACL was a direct target of and negatively regulated by miR-145-5p.…”

Section: Discussionmentioning

confidence: 62%

miR-145-5p Overexpression Inhibits the Proliferation, Migration and Invasion of Esophageal Carcinoma Cells by Targeting ABRACL

Fan

Chen

2020

Preprint

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Background: The study aimed to investigate the regulatory relationship between miR-145-5p and ABRACL, and tried to clarify the mechanisms underlying the proliferation, migration and invasion of esophageal cancer (EC) cells.Methods: Gene expression data related to EC were accessed from TCGA database and the “edgeR” package was used to screen the differentially expressed miRNA (DEmiRNAs) and genes (DEGs). TargetScan, miRDB and miRTarBase databases were used to predict potential targets for the target miRNA miR-145-5p. qRT-PCR and Western blot were performed to assess the expression of miR-145-5p and ABRACL in EC cells. Dual-luciferase reporter assay was performed for verification of the targeting relationship between miR-145-5p and ABRACL. Functional experiments including colony formation assay, Transwell migration and invasion assays were used to detect the proliferation, migration and invasion abilities of EC cells. Results: The expression of miR-145-5p was significantly decreased in EC, while ABRACL was remarkably increased. In addition, there was a negative correlation identified between miR-145-5p and ABRACL expression levels. Overexpressing miR-145-5p was able to suppress cell proliferation, migration and invasion, whereas silencing miR-145-5p posed an opposite effect. In the meantime, ABRACL was identified as a direct target of miR-145-5p by dual-luciferase reporter assay. Furthermore, miR-145-5p could inhibit the expression of ABRACL, in turn inhibiting the proliferation, migration and invasion of EC cells. Conclusion: miR-145-5p functions on the proliferation, migration and invasion of EC cells via targeting ABRACL, and it may be a novel therapeutic target for EC treatment.

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Section: Discussionmentioning

confidence: 62%

miR-145-5p Overexpression Inhibits the Proliferation, Migration and Invasion of Esophageal Carcinoma Cells by Targeting ABRACL

Fan

Chen

2020

Preprint

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“…These regions contain two independent F-actin binding domains, actin binding domain 1 and 2 (ABD1/ABD2) (Fogl et al, 2011). ABD1 (fragment 193–296) binds with higher affinity to F-actin when compared to ABD2.…”

Section: Localization and Activation Of Starsmentioning

confidence: 99%

“…ABD1 (fragment 193–296) binds with higher affinity to F-actin when compared to ABD2. ABD1 does not adopt a well-folded structure until it is bound to F-actin (Fogl et al, 2011), while ABD2 (fragment 294–375), the most C-terminal fragment, is independently folded (Fogl et al, 2011). It has been hypothesized that ABD1 could completely fulfill the actin-binding function of STARS in muscle, therefore, leaving ABD2 available for other potential functions within muscle (Fogl et al, 2011).…”

Section: Localization and Activation Of Starsmentioning

confidence: 99%

“…ABD1 does not adopt a well-folded structure until it is bound to F-actin (Fogl et al, 2011), while ABD2 (fragment 294–375), the most C-terminal fragment, is independently folded (Fogl et al, 2011). It has been hypothesized that ABD1 could completely fulfill the actin-binding function of STARS in muscle, therefore, leaving ABD2 available for other potential functions within muscle (Fogl et al, 2011). While STARS is predominantly cytosolic, we (Wallace et al, 2011) and others (Arai et al, 2002) have observed its location in the nucleus.…”

Section: Localization and Activation Of Starsmentioning

confidence: 99%

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The regulation and function of the striated muscle activator of rho signaling (STARS) protein

2012

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Healthy living throughout the lifespan requires continual growth and repair of cardiac, smooth, and skeletal muscle. To effectively maintain these processes muscle cells detect extracellular stress signals and efficiently transmit them to activate appropriate intracellular transcriptional programs. The striated muscle activator of Rho signaling (STARS) protein, also known as Myocyte Stress-1 (MS1) protein and Actin-binding Rho-activating protein (ABRA) is highly enriched in cardiac, skeletal, and smooth muscle. STARS binds actin, co-localizes to the sarcomere and is able to stabilize the actin cytoskeleton. By regulating actin polymerization, STARS also controls an intracellular signaling cascade that stimulates the serum response factor (SRF) transcriptional pathway; a pathway controlling genes involved in muscle cell proliferation, differentiation, and growth. Understanding the activation, transcriptional control and biological roles of STARS in cardiac, smooth, and skeletal muscle, will improve our understanding of physiological and pathophysiological muscle development and function.

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“…The size of the protein increased in the course of evolution from a short, 81 residue version called COSTARS [ 9 ] in the smallest known eukaryotes via a version of about 150 residues in insects and nematodes and just under 400 amino acids in vertebrates [ 10 ] ( S1 Fig ). The protein was shown to bind to F-actin [ 3 , 10 ], which was increased by its interaction with ABLIM-1/2 [ 11 ]. We were able to show that only its highly conserved C-terminus assumes a well-folded structure, while the rest of the protein is highly flexible and unfolded [ 10 ].…”

Section: Introductionmentioning

confidence: 99%

The Cardiac Stress Response Factor Ms1 Can Bind to DNA and Has a Function in the Nucleus

et al. 2015

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Ms1 (also known as STARS and ABRA) has been shown to act as an early stress response gene in processes as different as hypertrophy in skeletal and cardiac muscle and growth of collateral blood vessels. It is important for cardiac development in zebrafish and is upregulated in mouse models for cardiac hypertrophy as well as in human failing hearts. Ms1 possesses actin binding sites at its C-terminus and is usually found in the cell bound to actin filaments in the cytosol or in sarcomeres. We determined the NMR structure of the only folded domain of Ms1 comprising the second actin binding site called actin binding domain 2 (ABD2, residues 294–375), and found that it is similar to the winged helix-turn-helix fold adopted mainly by DNA binding domains of transcriptional factors. In vitro experiments show specific binding of this domain, in combination with a newly discovered AT-hook motif located N-terminally, to the sequence (). NMR and fluorescence titration experiments confirm that this motif is indeed bound specifically by the recognition helix. In neonatal rat cardiomyocytes endogenous Ms1 is found in the nucleus in a spotted pattern, reminiscent of PML bodies. In adult rat cardiomyocytes Ms1 is exclusively found in the sarcomere. A nuclear localisation site in the N-terminus of the protein is required for nuclear localisation. This suggests that Ms1 has the potential to act directly in the nucleus through specific interaction with DNA in development and potentially as a response to stress in adult tissues.

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A structural and functional dissection of the cardiac stress response factor MS1

Cited by 10 publications

References 38 publications

miR-145-5p Overexpression Inhibits the Proliferation, Migration and Invasion of Esophageal Carcinoma Cells by Targeting ABRACL

miR-145-5p Overexpression Inhibits the Proliferation, Migration and Invasion of Esophageal Carcinoma Cells by Targeting ABRACL

The regulation and function of the striated muscle activator of rho signaling (STARS) protein

The Cardiac Stress Response Factor Ms1 Can Bind to DNA and Has a Function in the Nucleus

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