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1. Biallelic variants in FLII cause pediatric cardiomyopathy by disrupting cardiomyocyte cell adhesion and myofibril organization

Author

Ruijmbeek, Claudine W.B., primary, Housley, Filomena, additional, Idrees, Hafiza, additional, Housley, Michael P., additional, Pestel, Jenny, additional, Keller, Leonie, additional, Lai, Jason K.H., additional, der Linde, Herma C. van, additional, Willemsen, Rob, additional, Piesker, Janett, additional, Al-Hassnan, Zuhair N., additional, Almesned, Abdulrahman, additional, Dalinghaus, Michiel, additional, den Bersselaar, Lisa M. van, additional, van Slegtenhorst, Marjon A., additional, Tessadori, Federico, additional, Bakkers, Jeroen, additional, van Ham, Tjakko J., additional, Stainier, Didier Y.R., additional, Verhagen, Judith M.A., additional, and Reischauer, Sven, additional

Published
2023
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2. Biallelic variants in FLII cause pediatric cardiomyopathy by disrupting cardiomyocyte cell adhesion and myofibril organization

Author

Ruijmbeek, Claudine Wb, Housley, Filomena, Idrees, Hafiza, Housley, Michael P, Pestel, Jenny, Keller, Leonie, Lai, Jason Kh, der Linde, Herma C van, Willemsen, Rob, Piesker, Janett, Al-Hassnan, Zuhair N, Almesned, Abdulrahman, Dalinghaus, Michiel, den Bersselaar, Lisa M van, van Slegtenhorst, Marjon A, Tessadori, Federico, Bakkers, Jeroen, van Ham, Tjakko J, Stainier, Didier Yr, Verhagen, Judith Ma, Reischauer, Sven, Ruijmbeek, Claudine Wb, Housley, Filomena, Idrees, Hafiza, Housley, Michael P, Pestel, Jenny, Keller, Leonie, Lai, Jason Kh, der Linde, Herma C van, Willemsen, Rob, Piesker, Janett, Al-Hassnan, Zuhair N, Almesned, Abdulrahman, Dalinghaus, Michiel, den Bersselaar, Lisa M van, van Slegtenhorst, Marjon A, Tessadori, Federico, Bakkers, Jeroen, van Ham, Tjakko J, Stainier, Didier Yr, Verhagen, Judith Ma, and Reischauer, Sven

Abstract

Pediatric cardiomyopathy (CM) represents a group of rare, severe disorders that affect the myocardium. To date, the etiology and mechanisms underlying pediatric CM are incompletely understood, hampering accurate diagnosis and individualized therapy development. Here, we identified biallelic variants in the highly conserved flightless-I (FLII) gene in 3 families with idiopathic, early-onset dilated CM. We demonstrated that patient-specific FLII variants, when brought into the zebrafish genome using CRISPR/Cas9 genome editing, resulted in the manifestation of key aspects of morphological and functional abnormalities of the heart, as observed in our patients. Importantly, using these genetic animal models, complemented with in-depth loss-of-function studies, we provided insights into the function of Flii during ventricular chamber morphogenesis in vivo, including myofibril organization and cardiomyocyte cell adhesion, as well as trabeculation. In addition, we identified Flii function to be important for the regulation of Notch and Hippo signaling, crucial pathways associated with cardiac morphogenesis and function. Taken together, our data provide experimental evidence for a role for FLII in the pathogenesis of pediatric CM and report biallelic variants as a genetic cause of pediatric CM.

Published
2023

3. Biallelic variants in FLII cause pediatric cardiomyopathy by disrupting cardiomyocyte cell adhesion and myofibril organization

Author

Cancer, Child Health, Cardiologie onderzoek 2, Onderzoek, Circulatory Health, Ruijmbeek, Claudine W.B., Housley, Filomena, Idrees, Hafiza, Housley, Michael P., Pestel, Jenny, Keller, Leonie, Lai, Jason K.H., van der Linde, Herma C., Willemsen, Rob, Piesker, Janett, Al-Hassnan, Zuhair N., Almesned, Abdulrahman, Dalinghaus, Michiel, van den Bersselaar, Lisa M., van Slegtenhorst, Marjon A., Tessadori, Federico, Bakkers, Jeroen, van Ham, Tjakko J., Stainier, Didier Y.R., Verhagen, Judith M.A., Reischauer, Sven, Cancer, Child Health, Cardiologie onderzoek 2, Onderzoek, Circulatory Health, Ruijmbeek, Claudine W.B., Housley, Filomena, Idrees, Hafiza, Housley, Michael P., Pestel, Jenny, Keller, Leonie, Lai, Jason K.H., van der Linde, Herma C., Willemsen, Rob, Piesker, Janett, Al-Hassnan, Zuhair N., Almesned, Abdulrahman, Dalinghaus, Michiel, van den Bersselaar, Lisa M., van Slegtenhorst, Marjon A., Tessadori, Federico, Bakkers, Jeroen, van Ham, Tjakko J., Stainier, Didier Y.R., Verhagen, Judith M.A., and Reischauer, Sven

Published
2023

4. A reverse signaling pathway downstream of Sema4A controls cell migration via Scrib

Author

Sun, Tianliang, primary, Yang, Lida, additional, Kaur, Harmandeep, additional, Pestel, Jenny, additional, Looso, Mario, additional, Nolte, Hendrik, additional, Krasel, Cornelius, additional, Heil, Daniel, additional, Krishnan, Ramesh K., additional, Santoni, Marie-Josée, additional, Borg, Jean-Paul, additional, Bünemann, Moritz, additional, Offermanns, Stefan, additional, Swiercz, Jakub M., additional, and Worzfeld, Thomas, additional

Published
2016
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6. A reverse signaling pathway downstream of Sema4A controls cell migration via Scrib.

Author

Tianliang Sun, Lida Yang, Kaur, Harmandeep, Pestel, Jenny, Looso, Mario, Heil, Daniel, Krishnan, Ramesh K., Swiercz, Jakub M., Nolte, Hendrik, Offermanns, Stefan, Worzfeld, Thomas, Krasel, Cornelius, Bünemann, Moritz, Santoni, Marie-Josée, and Borg, Jean-Paul

Subjects
*SEMAPHORINS, *CELL migration inhibition, *PLEXINS
Abstract

Semaphorins comprise a large family of ligands that regulate key cellular functions through their receptors, plexins. In this study, we show that the transmembrane semaphorin 4A (Sema4A) can also function as a receptor, rather than a ligand, and transduce signals triggered by the binding of Plexin-B1 through reverse signaling. Functionally, reverse Sema4A signaling regulates the migration of various cancer cells as well as dendritic cells. By combining mass spectrometry analysis with small interfering RNA screening, we identify the polarity protein Scrib as a downstream effector of Sema4A. We further show that binding of Plexin-B1 to Sema4A promotes the interaction of Sema4A with Scrib, thereby removing Scrib from its complex with the Rac/Cdc42 exchange factor βPIX and decreasing the activity of the small guanosine triphosphatase Rac1 and Cdc42. Our data unravel a role for Plexin-B1 as a ligand and Sema4A as a receptor and characterize a reverse signaling pathway downstream of Sema4A, which controls cell migration. [ABSTRACT FROM AUTHOR]

Published
2017
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7. A reverse signaling pathway downstream of Sema4A controls cell migration via Scrib.

Author

Sun T, Yang L, Kaur H, Pestel J, Looso M, Nolte H, Krasel C, Heil D, Krishnan RK, Santoni MJ, Borg JP, Bünemann M, Offermanns S, Swiercz JM, and Worzfeld T

Subjects
Animals, Genotype, HEK293 Cells, HeLa Cells, Humans, Intracellular Signaling Peptides and Proteins genetics, Mass Spectrometry, Membrane Proteins genetics, Mice, Inbred C57BL, Mice, Knockout, Neoplasm Invasiveness, Neoplasms genetics, Neoplasms pathology, Nerve Tissue Proteins metabolism, Phenotype, RNA Interference, Receptors, Cell Surface metabolism, Rho Guanine Nucleotide Exchange Factors metabolism, Semaphorins deficiency, Semaphorins genetics, Time Factors, Transfection, Tumor Suppressor Proteins genetics, cdc42 GTP-Binding Protein metabolism, rac GTP-Binding Proteins metabolism, Cell Movement, Dendritic Cells metabolism, Intracellular Signaling Peptides and Proteins metabolism, Membrane Proteins metabolism, Neoplasms metabolism, Semaphorins metabolism, Signal Transduction, Tumor Suppressor Proteins metabolism
Abstract

Semaphorins comprise a large family of ligands that regulate key cellular functions through their receptors, plexins. In this study, we show that the transmembrane semaphorin 4A (Sema4A) can also function as a receptor, rather than a ligand, and transduce signals triggered by the binding of Plexin-B1 through reverse signaling. Functionally, reverse Sema4A signaling regulates the migration of various cancer cells as well as dendritic cells. By combining mass spectrometry analysis with small interfering RNA screening, we identify the polarity protein Scrib as a downstream effector of Sema4A. We further show that binding of Plexin-B1 to Sema4A promotes the interaction of Sema4A with Scrib, thereby removing Scrib from its complex with the Rac/Cdc42 exchange factor βPIX and decreasing the activity of the small guanosine triphosphatase Rac1 and Cdc42. Our data unravel a role for Plexin-B1 as a ligand and Sema4A as a receptor and characterize a reverse signaling pathway downstream of Sema4A, which controls cell migration., (© 2017 Sun et al.)

Published
2017
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