ArticleThe Journal of biological chemistry2016
The Arf GTPase-activating Protein, ASAP1, Binds Nonmuscle Myosin 2A to Control Remodeling of the Actomyosin Network.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
22 citing papers in PubMed, 36 citations in OpenAlex.
- ASAP1 gene InDel variants are associated with enhanced goat resistance against Brucella infection.Animal bioscience · 2026Article
- Actin Binding to the BAR Domain and Arf GAP Activity of ASAP1 Coordinately Control Actin Stress Fibers and Focal Adhesions.Biology of the cell · 2025Article
- Aberrant expression of GTPase-activating protein ARAP1 triggers circular dorsal ruffles associated with malignancy in hepatocellular carcinoma Hep3B cells.Cell communication and signaling : CCS · 2025Article
- ASAP1 and ARF1 Regulate Myogenic Differentiation in Rhabdomyosarcoma by Modulating TAZ Activity.Molecular cancer research : MCR · 2025Article
- ARF: the most misunderstood GTPase I ever knew - why study ARF GAPs.Frontiers in molecular biosciences · 2025Review
- Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024Review
- Roles of G proteins and their GTPase-activating proteins in platelets.Bioscience reports · 2024Review
- Activated fibroblasts drive cellular interactions in end-stage pediatric hypertrophic cardiomyopathy.bioRxiv : the preprint server for biology · 2024Article
- The state of F-BAR domains as membrane-bound oligomeric platforms.Trends in cell biology · 2021Review
- The function of apolipoproteins L (APOLs): relevance for kidney disease, neurotransmission disorders, cancer and viral infection.The FEBS journal · 2021Review
- TheMolecular biology of the cell · 2020Article
- The BAR domain of the Arf GTPase-activating protein ASAP1 directly binds actin filaments.The Journal of biological chemistry · 2020Article
- APOL1 C-Terminal Variants May Trigger Kidney Disease through Interference with APOL3 Control of Actomyosin.Cell reports · 2020Article
- Article
- PEAK3/C19orf35 pseudokinase, a new NFK3 kinase family member, inhibits CrkII through dimerization.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Arf GAPs: A family of proteins with disparate functions that converge on a common structure, the integrin adhesion complex.Small GTPases · 2019Review
- ARF GTPases and their GEFs and GAPs: concepts and challenges.Molecular biology of the cell · 2019Review
- Arf GAPs and molecular motors.Small GTPases · 2019Review
- Arf GAPs as Regulators of the Actin Cytoskeleton-An Update.International journal of molecular sciences · 2019Review
- ARAP2 inhibits Akt independently of its effects on focal adhesions.Biology of the cell · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
ASAP1 regulates F-actin-based structures and functions, including focal adhesions (FAs) and circular dorsal ruffles (CDRs), cell spreading and migration. ASAP1 function requires its N-terminal BAR domain. We discovered that nonmuscle myosin 2A (NM2A) directly bound the BAR-PH tandem of ASAP1in vitro ASAP1 and NM2A co-immunoprecipitated and colocalized in cells. Knockdown of ASAP1 reduced colocalization of NM2A and F-actin in cells. Knockdown of ASAP1 or NM2A recapitulated each other's effects on FAs, cell migration, cell spreading, and CDRs. The NM2A-interacting BAR domain contributed to ASAP1 control of cell spreading and CDRs. Exogenous expression of NM2A rescued the effect of ASAP1 knockdown on CDRs but ASAP1 did not rescue NM2A knockdown defect in CDRs. Our results support the hypothesis that ASAP1 is a positive regulator of NM2A. Given other binding partners of ASAP1, ASAP1 may directly link signaling and the mechanical machinery of cell migration.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.