ArticleLife science alliance2019
Opposing functions of F-BAR proteins in neuronal membrane protrusion, tubule formation, and neurite outgrowth.
Article in Life science alliance, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- ADNP Functions During Early Brain Development and Their Relevance to ASD and ADNP Syndrome.International journal of molecular sciences · 2026Review
- F-BAR Proteins CIP4 and FBP17 Function in Cortical Neuron Radial Migration and Process Outgrowth.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025Article
- Membrane composition and curvature in SNX9-mediated actin polymerization.Molecular biology of the cell · 2025Article
- Distinct Bin/Amphiphysin/Rvs (BAR) family proteins may assemble on the same tubule to regulate membrane organizationHeliyon · 2024Article
- Filopodial protrusion driven by density-dependent Ena-TOCA-1 interactions.Journal of cell science · 2024Article
- Self-assembly of CIP4 drives actin-mediated asymmetric pit-closing in clathrin-mediated endocytosis.Nature communications · 2023Article
- The Mechanics and Thermodynamics of Tubule Formation in Biological Membranes.The Journal of membrane biology · 2021Review
- α-Linolenic acid induces clearance of Tau seeds via Actin-remodeling in Microglia.Molecular biomedicine · 2021Article
- Comparative Study of Curvature Sensing Mediated by F-BAR and an Intrinsically Disordered Region of FBP17.iScience · 2020Article
- Light-Inducible Generation of Membrane Curvature in Live Cells with Engineered BAR Domain Proteins.ACS synthetic biology · 2020Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
The F-BAR family of proteins play important roles in many cellular processes by regulating both membrane and actin dynamics. The CIP4 family of F-BAR proteins is widely recognized to function in endocytosis by elongating endocytosing vesicles. However, in primary cortical neurons, CIP4 concentrates at the tips of extending lamellipodia and filopodia and inhibits neurite outgrowth. Here, we report that the highly homologous CIP4 family member, FBP17, induces tubular structures in primary cortical neurons and results in precocious neurite formation. Through domain swapping and deletion experiments, we demonstrate that a novel polybasic region between the F-BAR and HR1 domains is required for membrane bending. Moreover, the presence of a poly-PxxP region in longer splice isoforms of CIP4 and FBP17 largely reverses the localization and function of these proteins. Thus, CIP4 and FBP17 function as an antagonistic pair to fine-tune membrane protrusion, endocytosis, and neurite formation during early neuronal development.
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Registered trials
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