ArticleBlood2015
FlnA binding to PACSIN2 F-BAR domain regulates membrane tubulation in megakaryocytes and platelets.
Article in Blood, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers, 1 of them a synthesis that pooled it.
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Who cites it
29 citing papers in PubMed, 1 synthesis or guideline pooled it, 58 citations in OpenAlex.
- Platelet-Related Variants Identified by Exomechip Meta-analysis in 157,293 Individuals.American journal of human genetics · 2016Pooled it
- PACSIN2 regulates mercaptopurine cytotoxicity and cellular biomechanics through Rac1 modulation in intestinal epithelial cells.Frontiers in pharmacology · 2026Article
- Increased RhoA pathway activation downstream of αIIbβ3/SRC contributes to heterozygous Bernard Soulier syndrome.Haematologica · 2025Article
- New insights of glycoprotein Ib-IX-V complex organization and glycoprotein Ibα in platelet biogenesis.Current opinion in hematology · 2024Review
- PACSIN2 regulates platelet integrin β1 hemostatic function.Journal of thrombosis and haemostasis : JTH · 2023Article
- A novel association between platelet filamin A and soluble N-ethylmaleimide sensitive factor attachment proteins regulates granule secretion.Research and practice in thrombosis and haemostasis · 2023Article
- Excessive serine from the bone marrow microenvironment impairs megakaryopoiesis and thrombopoiesis in Multiple Myeloma.Nature communications · 2023Article
- Platelets and Cardioprotection: The Role of Nitric Oxide and Carbon Oxide.International journal of molecular sciences · 2023Review
- A gain-of-function filamin A mutation in mouse platelets induces thrombus instability.Journal of thrombosis and haemostasis : JTH · 2022Article
- Fission yeast paxillin contains two Cdc15 binding motifs for robust recruitment to the cytokinetic ring.Molecular biology of the cell · 2022Article
- Multiple causal variants underlie genetic associations in humans.Science (New York, N.Y.) · 2022Article
- PACSIN proteins in vivo: Roles in development and physiology.Acta physiologica (Oxford, England) · 2022Review
- PSTPIP1-LYP phosphatase interaction: structural basis and implications for autoinflammatory disorders.Cellular and molecular life sciences : CMLS · 2022Article
- Filamin A in platelets: Bridging the (signaling) gap between the plasma membrane and the actin cytoskeleton.Frontiers in molecular biosciences · 2022Review
- The state of F-BAR domains as membrane-bound oligomeric platforms.Trends in cell biology · 2021Review
- Opposite Surfaces of the Cdc15 F-BAR Domain Create a Membrane Platform That Coordinates Cytoskeletal and Signaling Components for Cytokinesis.Cell reports · 2020Article
- Article
- Dynamin 2 is required for GPVI signaling and platelet hemostatic function in mice.Haematologica · 2020Article
- The intrinsically disordered region of the cytokinetic F-BAR protein Cdc15 performs a unique essential function in maintenance of cytokinetic ring integrity.Molecular biology of the cell · 2019Article
- New insights into cytoskeletal remodeling during platelet production.Journal of thrombosis and haemostasis : JTH · 2019Review
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Authors and funding
14 authors at 5 institutions in 3 countries.
Funding
Abstract
Bin-Amphiphysin-Rvs (BAR) and Fes-CIP4 homology BAR (F-BAR) proteins generate tubular membrane invaginations reminiscent of the megakaryocyte (MK) demarcation membrane system (DMS), which provides membranes necessary for future platelets. The F-BAR protein PACSIN2 is one of the most abundant BAR/F-BAR proteins in platelets and the only one reported to interact with the cytoskeletal and scaffold protein filamin A (FlnA), an essential regulator of platelet formation and function. The FlnA-PACSIN2 interaction was therefore investigated in MKs and platelets. PACSIN2 associated with FlnA in human platelets. The interaction required FlnA immunoglobulin-like repeat 20 and the tip of PACSIN2 F-BAR domain and enhanced PACSIN2 F-BAR domain membrane tubulation in vitro. Most human and wild-type mouse platelets had 1 to 2 distinct PACSIN2 foci associated with cell membrane GPIbα, whereas Flna-null platelets had 0 to 4 or more foci. Endogenous PACSIN2 and transfected enhanced green fluorescent protein-PACSIN2 were concentrated in midstage wild-type mouse MKs in a well-defined invagination of the plasma membrane reminiscent of the initiating DMS and dispersed in the absence of FlnA binding. The DMS appeared less well defined, and platelet territories were not readily visualized in Flna-null MKs. We conclude that the FlnA-PACSIN2 interaction regulates membrane tubulation in MKs and platelets and likely contributes to DMS formation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.