Pacsin 2 is required for the maintenance of a normal cardiac function in the developing mouse heart

Semmler, Judith; Kormann, Jan; Srinivasan, Sureshkumar Perumal; Köster, Annette; Sälzer, Daniel; Reppel, Michael; Hescheler, Jürgen; Plomann, Markus; Nguemo, Filomain

doi:10.1016/j.phrs.2017.10.004

Cited by 5 publications

(10 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Because loss of PACSIN2 caused only a moderate change in the electrophysiological properties of the ventricular myocytes, the authors suggest that PACSIN2 may play an important role in the regulation of the beating frequency of the developing heart by altering the atrial functions where the action potentials are initiated. The authors further propose that the alterations in the PACSIN2 knockout cardiomyocytes may result from improper targeting of ion channels to the plasma membrane 104 …”

Section: Pacsins In Muscle Biologymentioning

confidence: 99%

Section: Pacsins In Muscle Biologymentioning

confidence: 99%

“…In the adult PACSIN2 knockout mice, many cardiac genes are downregulated in the heart tissue but despite this, the knockout mice display normal heart morphology 104 . The authors mentioned, though, that the mice depleted of PACSIN2 show reduced running endurance, distance and speed compared to their wildtype counterparts 104 . Another study reported that supplementing the diet with antioxidants, namely vitamin‐E and α‐lipoic acid, induces transcriptional upregulation of PACSIN2, among several other genes, in adult male rat myocardial tissue after 14 weeks of treatment 105 .…”

Section: Pacsins In Muscle Biologymentioning

confidence: 99%

See 2 more Smart Citations

PACSIN proteins in vivo: Roles in development and physiology

Dumont

Lehtonen

2022

Acta Physiologica

View full text Add to dashboard Cite

Protein kinase C and casein kinase substrate in neurons (PACSINs), or syndapins (synaptic dynamin‐associated proteins), are a family of proteins involved in the regulation of cell cytoskeleton, intracellular trafficking and signalling. Over the last twenty years, PACSINs have been mostly studied in the in vitro and ex vivo settings, and only in the last decade reports on their function in vivo have emerged. We first summarize the identification, structure and cellular functions of PACSINs, and then focus on the relevance of PACSINs in vivo. During development in various model organisms, PACSINs participate in diverse processes, such as neural crest cell development, gastrulation, laterality development and neuromuscular junction formation. In mouse, PACSIN2 regulates angiogenesis during retinal development and in human, PACSIN2 associates with monosomy and embryonic implantation. In adulthood, PACSIN1 has been extensively studied in the brain and shown to regulate neuromorphogenesis, receptor trafficking and synaptic plasticity. Several genetic studies suggest a role for PACSIN1 in the development of schizophrenia, which is also supported by the phenotype of mice depleted of PACSIN1. PACSIN2 plays an essential role in the maintenance of intestinal homeostasis and participates in kidney repair processes after injury. PACSIN3 is abundant in muscle tissue and necessary for caveolar biogenesis to create membrane reservoirs, thus controlling muscle function, and has been linked to certain genetic muscular disorders. The above examples illustrate the importance of PACSINs in diverse physiological or tissue repair processes in various organs, and associations to diseases when their functions are disturbed.

show abstract

Section: Pacsins In Muscle Biologymentioning

confidence: 99%

Section: Pacsins In Muscle Biologymentioning

confidence: 99%

Section: Pacsins In Muscle Biologymentioning

confidence: 99%

See 1 more Smart Citation

PACSIN proteins in vivo: Roles in development and physiology

Dumont

Lehtonen

2022

Acta Physiologica

View full text Add to dashboard Cite

show abstract

“…In particular, animal models for the ubiquitously expressed PACSIN2 have only recently been described. Loss of PACSIN2 in mice does not affect viability or fertility and the animals appear generally healthy ( Malinova et al, 2021 ; Postema et al, 2019 ; Semmler et al, 2018 ). However, a number of tissue-specific phenotypes have been reported in the PACSIN2 knockouts, namely effects upon microvillar structure in the intestine ( Postema et al, 2019 ), reduced blood vessel sprouting in the retina ( Malinova et al, 2021 ), and delayed cardiomyocyte development ( Semmler et al, 2018 ).…”

Section: Introductionmentioning

confidence: 99%

“…Loss of PACSIN2 in mice does not affect viability or fertility and the animals appear generally healthy ( Malinova et al, 2021 ; Postema et al, 2019 ; Semmler et al, 2018 ). However, a number of tissue-specific phenotypes have been reported in the PACSIN2 knockouts, namely effects upon microvillar structure in the intestine ( Postema et al, 2019 ), reduced blood vessel sprouting in the retina ( Malinova et al, 2021 ), and delayed cardiomyocyte development ( Semmler et al, 2018 ). The former two phenotypes were attributed to endocytic trafficking defects, either defective endocytic vesicle formation at the apical membrane ( Malinova et al, 2021 ), or defective cadherin trafficking ( Malinova et al, 2021 ), respectively.…”

Section: Introductionmentioning

confidence: 99%

Pacsin2 is required for endocytosis in the zebrafish pronephric tubule

et al. 2022

View full text Add to dashboard Cite

Endocytosis mediates the cellular uptake of numerous molecules from the extracellular space and is a fundamentally important process. In the renal proximal tubule, the scavenger receptor megalin and its co-receptor cubilin mediate endocytosis of low molecular weight proteins from the renal filtrate. However, the extent to which megalin endocytosis relies on different components of the trafficking machinery remains relatively poorly defined in vivo. In this study, we identify a functional requirement for the F-BAR protein pacsin2 in endocytosis in the renal proximal tubule of zebrafish larvae. Pacsin2 is expressed throughout development and in all zebrafish tissues, similar to the mammalian orthologue. Within renal tubular epithelial cells, pacsin2 is enriched at the apical pole where it is localised to endocytic structures. Loss of pacsin2 results in reduced endocytosis within the proximal tubule, which is accompanied by a reduction in the abundance of megalin and endocytic organelles. Our results indicate that pacsin2 is required for efficient endocytosis in the proximal tubule, where it likely cooperates with other trafficking machinery to maintain endocytic uptake and recycling of megalin.

show abstract