Affinage

BASP1

Brain acid soluble protein 1 · UniProt P80723

Length
227 aa
Mass
22.7 kDa
Annotated
2026-04-28
100 papers in source corpus 39 papers cited in narrative 39 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

BASP1 is an N-terminally myristoylated, intrinsically disordered protein that functions as a membrane-associated regulator of actin dynamics and PIP2 signaling in neurons and as a nuclear transcriptional corepressor controlling differentiation and tumor suppression. At the plasma membrane, myristoylation targets BASP1 to cholesterol-rich lipid rafts where it oligomerizes, clusters PIP2, promotes subplasmalemmal actin accumulation and neurite outgrowth, and inhibits synaptojanin-1 phosphatase and dynamin I GTPase to modulate synaptic vesicle cycling (PMID:10871285, PMID:10871284, PMID:21932368, PMID:29604406). In the nucleus, myristoylated BASP1 binds PIP2 and cholesterol to recruit HDAC1, prohibitin, and BRG1 to WT1 target gene promoters, removing active histone marks (H3K9ac, H3K4me3) and enforcing transcriptional repression that maintains differentiated cell states, as demonstrated in vivo by conditional knockout in taste receptor cells and podocytes (PMID:22939983, PMID:24166496, PMID:34266955, PMID:31167803). BASP1 also suppresses oncogenic transformation by displacing calmodulin from Myc to destabilize it, interacts with ERα to control tamoxifen-responsive gene programs in breast cancer, suppresses canonical WNT/MYC signaling via β-catenin interaction, and is required in myeloid cells for NLRP3 inflammasome activation and pro-inflammatory cytokine production (PMID:31944520, PMID:28492543, PMID:41785318, PMID:37505219).

Mechanistic history

Synthesis pass · year-by-year structured walk · 18 steps
  1. 1990 High

    The identification of BASP1 as an N-terminally myristoylated PKC substrate established that the protein is membrane-associated via lipid modification and subject to phosphorylation-dependent regulation at Ser-6.

    Evidence In vitro PKC assay, cDNA cloning, immunofluorescence in cultured cells

    PMID:2148567

    Open questions at the time
    • No cellular function assigned
    • In vivo phosphorylation stoichiometry unknown
  2. 1994 High

    Discovery that calmodulin binding and PKC phosphorylation are mutually exclusive regulatory switches on BASP1 revealed a signaling logic whereby Ca²⁺/calmodulin and PKC compete for control of the same N-terminal effector domain.

    Evidence In vitro PKC assay with deletion mutants, fluorescence-based calmodulin binding, liposome binding assays

    PMID:8034714 PMID:8193160

    Open questions at the time
    • Physiological contexts in which switching occurs were undefined
    • Downstream consequences of each state unknown
  3. 1997 High

    Localization of BASP1 to lipid rafts and demonstration that the effector domain drives shared morphological changes with GAP-43 and MARCKS established BASP1 as a member of a functional family (GMC proteins) that remodel the cell surface via acylation-dependent membrane targeting.

    Evidence Triton-insoluble fractionation, double-labeling immunocytochemistry, deletion/fusion transfection

    PMID:9030206 PMID:9344590

    Open questions at the time
    • Direct lipid-binding specificity not yet mapped
    • Mechanism of actin regulation unknown
  4. 1999 High

    Demonstration that cholesterol is required for BASP1 raft association and that myristoylation is essential for calmodulin binding defined the N-terminal myristoyl group as a bifunctional anchor mediating both membrane insertion and protein–protein interaction.

    Evidence Methyl-β-cyclodextrin cholesterol extraction, liposome reconstitution, myristoylated vs. non-myristoylated recombinant protein binding assays

    PMID:10207003 PMID:10409698

    Open questions at the time
    • Cholesterol-binding site not mapped
    • How calmodulin and membrane binding are coordinated in cells was unknown
  5. 2000 High

    Genetic loss-of-function in mice and PI(4,5)P2 clustering assays established that BASP1 promotes neurite outgrowth and nerve sprouting by retaining PIP2 at the plasma membrane and driving subplasmalemmal actin accumulation, answering the question of what cellular process the GMC effector domain serves.

    Evidence BASP1 knockout mice, cultured sensory neurons, PIP2 retention assays, PC12 neurite outgrowth, transgenic rescue

    PMID:10871284 PMID:10871285

    Open questions at the time
    • Whether PIP2 clustering directly causes actin accumulation or acts through intermediaries was unresolved
    • Nuclear function not yet suspected
  6. 2003 High

    Biophysical reconstitution showing that myristoylation-dependent oligomerization of BASP1 is required for selective cholesterol-rich domain binding resolved why monomeric BASP1 does not show lipid selectivity and introduced self-association as a regulatory step.

    Evidence Analytical ultracentrifugation, AFM, FRET-based liposome binding

    PMID:12718518 PMID:12922169

    Open questions at the time
    • Oligomeric stoichiometry in cells unknown
    • Whether oligomerization is regulated by calmodulin or phosphorylation in vivo was untested
  7. 2004 High

    The crystal structure of the myristoylated N-terminal peptide bound to Ca²⁺/calmodulin revealed a novel binding mode in which the myristoyl chain inserts into a hydrophobic tunnel of calmodulin, providing atomic-level explanation for the myristoylation requirement for calmodulin binding and the mutual exclusivity with membrane insertion.

    Evidence X-ray crystallography of myristoylated peptide–Ca²⁺/CaM complex

    PMID:14765114

    Open questions at the time
    • Full-length BASP1 structure unavailable
    • Dynamics of myristoyl switching in cells unresolved
  8. 2004 High

    Identification of BASP1 as a WT1 transcriptional cosuppressor by nuclear co-immunoprecipitation and functional reporter assays was the first evidence that BASP1 operates in the nucleus to regulate gene expression, fundamentally expanding its functional repertoire beyond membrane biology.

    Evidence Co-IP from nuclear extracts, reporter assays, siRNA knockdown

    PMID:14701728

    Open questions at the time
    • Mechanism of nuclear import unknown
    • How membrane-associated BASP1 reaches the nucleus unresolved
  9. 2008 High

    ChIP-based demonstration that the WT1–BASP1 complex dynamically occupies promoters (Bak, c-myc, podocalyxin) during differentiation, with sumoylation regulating BASP1 promoter dissociation, established that BASP1 corepressor function is post-translationally tuned during cell fate decisions.

    Evidence ChIP in podocyte precursor cells, differentiation assays

    PMID:19050011

    Open questions at the time
    • SUMO site(s) on BASP1 not mapped
    • Whether sumoylation directly weakens DNA/chromatin association or acts indirectly was unknown
  10. 2009 High

    BASP1 was shown to suppress v-Myc-induced transformation through its N-terminal myristoylated effector domain, and Myc itself suppresses BASP1 expression, establishing a reciprocal antagonism between BASP1 and oncogenic Myc.

    Evidence Retroviral co-expression, transformation assays (focus formation, soft agar), deletion mutagenesis, RT-PCR

    PMID:19297618

    Open questions at the time
    • Molecular mechanism of Myc inhibition not yet identified (calmodulin displacement discovered later)
  11. 2012 High

    The requirement for myristoylation of nuclear BASP1 in PIP2 binding, HDAC1 recruitment, and promoter-level histone deacetylation unified the lipid-binding and transcriptional corepressor functions, showing that the same lipid-interaction mechanism that clusters PIP2 at membranes also operates at chromatin.

    Evidence Myristoylation-dead mutant, PIP2 binding assay, Co-IP with HDAC1, ChIP for PIP2 and HDAC1 at target promoters

    PMID:22939983

    Open questions at the time
    • Source of nuclear PIP2 and how lipid reaches chromatin unclear
    • Whether HDAC1 binding is direct or PIP2-bridged was not resolved
  12. 2013 High

    Identification of prohibitin and BRG1 as BASP1-dependent components of the WT1 repression complex, with BASP1 required for BRG1 recruitment and CBP displacement, expanded the corepressor mechanism to include chromatin remodeling beyond simple deacetylation.

    Evidence Reciprocal Co-IP, ChIP for prohibitin/BRG1/CBP, knockdown experiments

    PMID:24166496

    Open questions at the time
    • Whether prohibitin directly contacts BASP1 or requires PIP2/cholesterol bridging unknown
    • Stoichiometry and assembly order of the complex unresolved
  13. 2017 High

    Discovery that BASP1 interacts with ERα and controls ~40% of tamoxifen-regulated genes extended the corepressor function beyond WT1 to a second nuclear receptor, linking BASP1 to breast cancer therapeutic response.

    Evidence Co-IP of BASP1 with ERα, siRNA knockdown, genome-wide expression analysis, cell viability assays

    PMID:28492543

    Open questions at the time
    • Whether BASP1 employs the same PIP2/cholesterol/HDAC mechanism for ERα repression as for WT1 was not tested
  14. 2019 High

    Conditional BASP1 knockout in taste receptor cells provided the first in vivo proof that WT1–BASP1 transcriptional repression is required to maintain differentiated cell identity by silencing Wnt and Shh pathway genes.

    Evidence Conditional KO mouse, ChIP, gene expression analysis, functional taste assays

    PMID:31167803

    Open questions at the time
    • Whether BASP1 loss fully recapitulates WT1 loss in this context was not compared
    • Relevance to other terminally differentiated tissues untested
  15. 2020 High

    The mechanism by which BASP1 suppresses Myc was resolved: BASP1's effector domain displaces calmodulin from Myc, destabilizing Myc protein, and ectopic calmodulin rescues transformation, demonstrating that calmodulin sequestration is the primary anti-Myc mechanism.

    Evidence Co-IP of effector peptide with CaM, competition assays, Myc stability assays, CaM rescue of transformation

    PMID:31944520

    Open questions at the time
    • Whether this mechanism operates in non-transformed cells unknown
    • Structural basis of CaM–Myc interaction not defined
  16. 2021 High

    Demonstration that BASP1 directly recruits cholesterol to WT1 target promoters through a conserved cholesterol interaction motif, and that disruption of this motif ablates transcriptional repression and chromatin compaction, added cholesterol as a second nuclear lipid cofactor (alongside PIP2) essential for BASP1 corepressor function.

    Evidence Cholesterol binding assays with mutants, ChIP for cholesterol at promoters, cholesterol biosynthesis inhibitors, ATAC-seq

    PMID:34266955

    Open questions at the time
    • How cholesterol reaches the nucleus and is loaded onto BASP1 is unknown
    • Whether PIP2 and cholesterol act at the same or distinct promoter subsets unresolved
  17. 2022 High

    Genome-wide dissection revealed that BASP1 removes H3K9ac and H3K4me3 in a myristoylation-dependent manner but places H3K27me3 independently of myristoylation, demonstrating that BASP1 employs mechanistically distinct lipidation-dependent and lipidation-independent pathways for chromatin modification.

    Evidence Myristoylation-dead mutant, ChIP for histone marks, RNA-seq, ATAC-seq

    PMID:35982799

    Open questions at the time
    • Identity of H3K27 methyltransferase recruited by non-myristoylated BASP1 unknown
    • Whether lipidation-independent pathway involves a different protein complex unresolved
  18. 2023 High

    Myeloid-specific BASP1 deletion attenuated NASH by impairing NLRP3 inflammasome activation and cytokine secretion, revealing that BASP1's role extends to innate immune inflammatory signaling beyond its known neuronal and WT1-dependent functions.

    Evidence Myeloid-specific conditional KO mice, diet-induced NASH, scRNA-seq, inflammasome assays

    PMID:37505219

    Open questions at the time
    • Molecular mechanism linking BASP1 to NLRP3 activation unclear—whether WT1/transcriptional repression or membrane/PIP2 function is involved is untested

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key unresolved questions include: how BASP1 partitions between membrane and nuclear pools, the mechanism of nuclear import, the structural basis for full-length BASP1 function, the relationship between oligomerization state and transcriptional vs. membrane activities, and whether the lipid cofactor (PIP2/cholesterol) mechanism underlies BASP1 functions in inflammation and Wnt suppression.
  • No structural model of full-length BASP1 exists
  • Nuclear import mechanism completely uncharacterized
  • Relative contribution of membrane vs. nuclear BASP1 in disease contexts unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0140110 transcription regulator activity 7 GO:0008289 lipid binding 6 GO:0008092 cytoskeletal protein binding 3 GO:0098772 molecular function regulator activity 3
Localization
GO:0005886 plasma membrane 5 GO:0005634 nucleus 4 GO:0005829 cytosol 1
Pathway
R-HSA-74160 Gene expression (Transcription) 7 R-HSA-4839726 Chromatin organization 4 R-HSA-162582 Signal Transduction 3 R-HSA-1266738 Developmental Biology 2 R-HSA-168256 Immune System 1
Partners
CALM1DNM1ESR1HDAC1PHBSMARCA4SYNJ1WT1
Complex memberships
WT1-BASP1-HDAC1-prohibitin-BRG1 corepressor complex

Evidence

Reading pass · 39 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1990 CAP-23/BASP1 is a substrate for protein kinase C (PKC) in vitro, and is phosphorylated in a PMA-sensitive manner in cultured cells; the protein has a PKC phosphorylation site at Ser-6 and is N-terminally myristoylated, which mediates its membrane association. In vitro PKC assay, cDNA cloning and sequence analysis, Western blot and immunofluorescence in cultured cells The Journal of cell biology High 2148567
1994 NAP-22/BASP1 is phosphorylated by PKC at Ser6; calmodulin inhibits this phosphorylation in a dose-dependent manner, and phosphorylation of NAP-22 abolishes its association with calmodulin. In vitro PKC phosphorylation assay using deleted mutants expressed in E. coli; fluorescence-based calmodulin binding assay The Journal of biological chemistry High 8034714
1994 NAP-22/BASP1 is N-terminally myristoylated and this myristoylation mediates its binding to liposomes; the protein lacks transmembrane regions but is membrane-associated via myristoylation and a polybasic N-terminal domain. Baculovirus expression system demonstrating myristoylation; E. coli expression with liposome binding assay Biochimica et biophysica acta High 8193160
1997 CAP-23/BASP1, GAP-43, and MARCKS accumulate at shared surface-associated structures in cells and induce the same range of characteristic changes in cell morphology and cell surface activities (blebs, filopodia, actin dynamics); these activities required acylation-mediated membrane targeting plus a GMC-type effector domain sequence. Double-labeling immunocytochemistry, transfection with deletion/fusion constructs, morphological analysis Experimental cell research High 9344590
1997 NAP-22/BASP1 is localized in a Triton-insoluble low-density membrane fraction (lipid raft) of rat brain together with GAP-43, trimeric G proteins, GPI-anchored proteins, and tyrosine kinases (src, fyn). Subcellular fractionation, Western blot Biochimica et biophysica acta Medium 9030206
1999 NAP-22/BASP1 localization to neuronal membrane raft is cholesterol-dependent; cholesterol extraction with methyl-β-cyclodextrin solubilizes NAP-22, and purified NAP-22 binds liposomes containing phosphatidylcholine and cholesterol in a cholesterol concentration-dependent manner; calmodulin inhibits this lipid binding. Cholesterol extraction (methyl-β-cyclodextrin), liposome binding assay, fluorescence-based calmodulin inhibition assay The Journal of biological chemistry High 10409698
1999 The calmodulin-binding domain of CAP-23/NAP-22 requires N-terminal myristoylation: only myristoylated (not non-myristoylated) recombinant protein and myristoylated N-terminal peptides bind calmodulin; the binding site is the myristoyl moiety plus a nine-amino-acid N-terminal basic domain; PKC phosphorylation of Ser5 abolishes calmodulin binding; PKC phosphorylation itself is myristoylation-dependent. Recombinant protein expression in E. coli (myristoylated and non-myristoylated forms), synthetic peptide binding assays, in vitro PKC phosphorylation assay The Journal of biological chemistry High 10207003
2000 CAP-23/BASP1, GAP-43, and MARCKS (GMC) promote retention and clustering of PI(4,5)P2 at plasma membrane rafts; this depends on the basic effector domain (ED) of these proteins; deletion of the ED creates dominant inhibitors of plasmalemmal PI(4,5)P2 modulation; GMC augment NGF- and substrate-induced peripheral actin structures and neurite outgrowth in PC12 cells; dominant-negative GAP-43(ΔED) inhibits peripheral nerve regeneration in transgenic mice. Transfection with ED deletion constructs, PI(4,5)P2 retention assays, PC12 neurite outgrowth assay, transgenic mouse nerve regeneration model The Journal of cell biology High 10871285
2000 CAP-23/BASP1 knockout mice show a pronounced defect in stimulus-induced nerve sprouting at the adult neuromuscular junction; cultured sensory neurons lacking CAP-23 show striking alterations in neurite outgrowth phenocopied by cytochalasin D, indicating BASP1 promotes subplasmalemmal actin cytoskeleton accumulation. GAP-43 can functionally substitute for CAP-23 in vivo (knockin mice). Knockout and knockin mouse genetics, nerve sprouting assay, primary neuronal culture with cytochalasin D, transgenic rescue experiments The Journal of cell biology High 10871284
2000 NAP-22/BASP1 is sorted preferentially into the axon of developing hippocampal neurons and co-localizes with tau and VAMP-2; its axonal localization is later than GAP-43, correlating with synapse maturation rather than initial axon outgrowth. Immunofluorescence and confocal microscopy of cultured hippocampal neurons at defined developmental stages, co-localization with tau, MAP-2, and VAMP-2 Neuroscience research Medium 10958980
2002 NAP-22/BASP1 binds cholesterol, phosphatidylethanolamine (PE), and polyphosphoinositides in liposome assays; N-terminal myristoylation is essential for liposome binding; the lipid-binding region resides within the N-terminal 60 amino acids; in COS7 cells NAP-22 localizes to a Triton-insoluble low-density fraction co-localizing with PE and cholesterol. Liposome binding assay using eukaryotic and bacterial expression systems, C-terminal deletion constructs, immunofluorescence in COS7 cells Journal of neuroscience research High 12271466
2003 Native myristoylated NAP-22/BASP1 binds to cholesterol-rich raft-like domains in planar-supported lipid monolayers and resists nonionic detergent extraction; demyristoylated NAP-22 does not bind these domains; the protein shows very low lateral mobility, suggesting cholesterol binding and inter-NAP-22 interactions reduce its diffusion. Fluorescence microscopy on planar-supported lipid monolayers, methyl-β-cyclodextrin extraction, lateral mobility measurement Biochemistry High 12718518
2003 NAP-22/BASP1 self-associates into oligomers in solution; myristoylation is required for oligomerization; oligomers bind specifically to cholesterol-rich membrane domains, whereas monomers do not show lipid selectivity. Oligomerization is a rapidly reversible equilibrium followed by slower irreversible aggregation. Sedimentation velocity and sedimentation equilibrium ultracentrifugation, atomic force microscopy, fluorescence resonance energy transfer (FRET) liposome binding Biochimica et biophysica acta High 12922169
2004 BASP1 is a transcriptional cosuppressor for the Wilms' tumor suppressor WT1: BASP1 associates with WT1 in the nuclei of cells co-expressing both proteins, confers cosuppressor activity in transfection assays, and elimination of endogenous BASP1 augments WT1-mediated transcriptional activation. Co-immunoprecipitation from nuclear extracts, transfection/reporter assays, siRNA knockdown of endogenous BASP1 Molecular and cellular biology High 14701728
2004 Crystal structure of myristoylated CAP-23/NAP-22 N-terminal domain complexed with Ca2+/calmodulin reveals that the myristoyl moiety inserts into a hydrophobic tunnel formed by the N- and C-terminal lobes of calmodulin — a novel mode of calmodulin binding requiring both the myristoyl group and specific N-terminal residues. X-ray crystallography of the myristoylated peptide–Ca2+/CaM complex The EMBO journal High 14765114
2004 A myristoylated N-terminal peptide of NAP-22 causes cholesterol-dependent sequestration of PI(4,5)P2 into membrane domains, as shown by fluorescence quenching of BODIPY-labeled PI(4,5)P2 in cholesterol-containing bilayers. Fluorescence spectroscopy and total internal reflectance fluorescence (TIRF) microscopy on defined lipid bilayers The Biochemical journal High 14989697
2008 Dynamic WT1-BASP1 complex occupies promoters of target genes (Bak, c-myc, podocalyxin) in podocyte precursor cells as shown by chromatin immunoprecipitation; during differentiation, BASP1 occupancy at the podocalyxin promoter is reduced while WT1 remains, correlating with gene upregulation; regulation of BASP1 promoter occupancy involves sumoylation of BASP1. Chromatin immunoprecipitation (ChIP), differentiation assays in podocyte precursor cell line Nucleic acids research High 19050011
2008 BASP1-induced neurite outgrowth requires N-terminal myristoylation (Gly1 mutation abolishes effect) but is independent of Ser5 phosphorylation; BASP1 and GAP-43 can substitute for each other for NCAM-independent neurite outgrowth but not for NCAM-dependent outgrowth; BASP1 acts through a pathway distinct from FGFR, Src, PKC, and GSK3β. Overexpression and site-directed mutagenesis in PC12E2 cells and primary hippocampal neurons; pharmacological inhibitors; dominant-negative constructs Journal of neuroscience research High 18438920
2009 BASP1 inhibits v-Myc-induced cell transformation; the basic N-terminal domain containing the myristoylation site, calmodulin-binding domain, and putative NLS is essential for this inhibitory function; BASP1 prevents Myc-mediated transcriptional activation/repression of known Myc target genes; BASP1 expression is specifically suppressed by v-myc oncogene. Retroviral co-expression of BASP1 and v-myc, ectopic BASP1 expression, transformation assays (focus formation, soft agar), deletion mutagenesis, RT-PCR for Myc target genes Proceedings of the National Academy of Sciences of the United States of America High 19297618
2009 NAP-22/BASP1 interacts with the actin-capping protein CapZ via pull-down assay; the N-terminal myristoyl moiety of NAP-22 is not required for CapZ binding; NAP-22 does not affect the actin nucleation activity of CapZ in vitro. Pull-down assay with brain-derived NAP-22 on Sepharose, mass spectrometry identification, Western blot confirmation, in vitro binding with bacterially expressed proteins, actin nucleation assay Journal of neuroscience research Medium 19267422
2010 BASP1 promotes apoptosis in tubular epithelial cells: overexpression induces cell death with apoptotic features; siRNA knockdown protects cells from apoptosis induced by serum deprivation, high glucose, and pro-inflammatory cytokines; in apoptotic cells BASP1 re-localizes from normal distribution to co-localize with actin at the cell periphery. BASP1 overexpression and siRNA knockdown in human tubular epithelial cells, flow cytometry for apoptosis, confocal microscopy for localization Journal of the American Society of Nephrology : JASN High 20110383
2011 BASP1 suppresses WT1-mediated transcriptional activation at WT1 target genes in K562 cells and is recruited to WT1-binding sites; WT1 and BASP1 together divert K562 cell differentiation toward a neuronal-like morphology with arborization and expression of neurite outgrowth genes. ChIP, reporter assays, siRNA knockdown, PMA-induced differentiation assay, morphological analysis The Biochemical journal High 21269271
2011 NAP-22/BASP1 interacts with synaptojanin-1 (identified by pull-down and LC-MS/MS); NAP-22 inhibits the phosphatase activity of synaptojanin-1 toward PIP2 in a dose-dependent manner, suggesting a role in regulating PIP2 levels during synaptic vesicle endocytosis. Pull-down assay, LC-MS/MS identification, Western blot confirmation, in vitro phosphatase activity assay Journal of neuroscience research Medium 21932368
2012 Transcriptional repression by WT1-BASP1 requires N-terminal myristoylation of BASP1; myristoylated BASP1 binds nuclear PIP2 and recruits PIP2 to promoters of WT1 target genes; BASP1 myristoylation and PIP2 association are required for BASP1-HDAC1 interaction and HDAC1 recruitment to promoters, leading to histone deacetylation and transcriptional repression. Myristoylation-dead BASP1 mutant, PIP2 binding assay, Co-IP of BASP1 with HDAC1, ChIP for PIP2 and HDAC1 at target promoters, reporter assays Cell reports High 22939983
2013 Prohibitin is part of the WT1-BASP1 transcriptional repression complex; prohibitin interacts with BASP1, co-localizes with BASP1 in the nucleus, and is recruited to promoters of WT1 target genes in a BASP1-dependent manner; prohibitin and BASP1 cooperate to recruit chromatin remodeling factor BRG1 to WT1-responsive promoters and displace CBP; this complex is also required for PIP2 and HDAC1 recruitment. Co-immunoprecipitation, co-localization by immunofluorescence, ChIP for prohibitin/BRG1/CBP/HDAC1/PIP2, knockdown experiments Oncogene High 24166496
2013 NAP-22/BASP1 interacts with glutamic acid decarboxylase (GAD65 and GAD67) by pull-down; interaction confirmed in vitro with bacterially expressed proteins; NAP-22 partially co-localizes with GAD65 and GAD67 in cultured neurons; NAP-22 binding does not affect GAD enzymatic activity. Pull-down with brain-derived NAP-22, LC-MS/MS identification, in vitro binding with bacterially expressed GST-GAD fusions, immunofluorescence co-localization, GAD enzymatic activity assay Neuroscience letters Medium 23376695
2017 BASP1 interacts with oestrogen receptor α (ERα); in breast cancer cells this interaction is enhanced by tamoxifen; BASP1 acts as a selectivity factor controlling ~40% of tamoxifen-regulated genes including tamoxifen-resistance genes; BASP1 enhances the antitumourigenic effects of tamoxifen. Co-immunoprecipitation of BASP1 with ERα, siRNA knockdown of BASP1, genome-wide gene expression analysis, cell viability and growth assays Cell death & disease High 28492543
2018 NAP-22/BASP1 interacts with dynamin I; NAP-22 inhibits the GTPase activity of dynamin I and this inhibition is reversed by calmodulin; NAP-22 also inhibits the activation of dynamin GTPase by acidic phospholipids (phosphatidylserine). Affinity pull-down screening with NAP-22 as bait, mass spectrometry, Western blot, in vitro GTPase activity assay Neuroscience letters Medium 29604406
2019 The WT1-BASP1 complex is required in vivo to maintain the differentiated state of taste receptor cells; conditional BASP1 knockout in mice de-represses WT1-dependent target genes from Wnt and Shh pathways normally active only in undifferentiated cells, leading to altered composition and function of adult taste cells. Conditional knockout mouse model (BASP1 floxed), ChIP, gene expression analysis, functional taste cell assays Life science alliance High 31167803
2020 The BASP1 effector domain (11 amino acids) interacts with calmodulin (CaM) and displaces v-Myc from CaM; excess BASP1 or synthetic BASP1 effector domain peptide decreases v-Myc protein stability; ectopic CaM rescues v-Myc transformation activity suppressed by BASP1, indicating BASP1-mediated CaM withdrawal from v-Myc is a key mechanism of inhibition. Co-immunoprecipitation of BASP1 effector peptide with CaM, competition assays, v-Myc stability assay, cell transformation rescue by ectopic CaM Molecular oncology High 31944520
2020 Membrane-bound BASP1 increases EGFR signaling and stabilizes EGFR protein by facilitating its escape from ubiquitin-proteasome degradation; EGFR activation reciprocally recruits more BASP1 to the plasma membrane, forming a positive feedback loop; this interaction promotes brain metastatic lung cancer progression. Tyrosine kinase activity assays, Co-IP, ubiquitination assays, in vitro and in vivo functional assays in lung cancer cells Theranostics Medium 33042262
2021 BASP1 interacts with cholesterol in the cell nucleus through a conserved cholesterol interaction motif; BASP1 directly recruits cholesterol to the promoter regions of WT1 target genes; mutation of the cholesterol interaction motif or cholesterol biosynthesis inhibitors ablate BASP1 transcriptional repressor function and BASP1-dependent chromatin remodeling. Cholesterol binding assays with BASP1 mutants, ChIP for cholesterol at promoters, pharmacological inhibition of cholesterol biosynthesis, reporter assays, ATAC-seq for chromatin accessibility Proceedings of the National Academy of Sciences of the United States of America High 34266955
2021 BASP1 promotes podocyte apoptosis in diabetic nephropathy via co-repression with WT1 to activate the p53 pathway; BASP1-specific deletion in podocytes protects against podocyte injury; BASP1 promotes actin cytoskeleton rearrangements and p53 pathway activation in podocytes. Podocyte-specific BASP1 conditional knockout mice, BASP1 knockdown and overexpression in cultured podocytes, Western blot for p53 pathway components, flow cytometry for apoptosis Acta physiologica (Oxford, England) High 33615732
2021 Truncated YY1 (YY1B) interacts with BASP1 through a 339KLK341 motif in YY1; mutation of this motif abrogates BASP1 interaction and YY1B-mediated inhibition of SMC proliferation; BASP1 overexpression independently inhibits SMC but not endothelial cell proliferation and migration; BASP1 siRNA partially rescues SMC from YY1B-mediated growth inhibition. GST pull-down with SMC lysates, mass spectrometry identification of BASP1, overexpression and siRNA experiments, carotid balloon injury model Cardiovascular research Medium 33508088
2022 BASP1 mediates removal of active histone marks H3K9ac and H3K4me3 at WT1 target genes in a myristoylation-dependent manner, while placement of repressive H3K27me3 by BASP1 does not require myristoylation; BASP1 regulates chromatin accessibility and the activity of multiple transcription factors; ~50% of BASP1 target genes show lipidation-dependent chromatin compaction. BASP1 myristoylation-dead mutant, ChIP for histone modifications, RNA-seq, ATAC-seq iScience High 35982799
2023 Myeloid-specific inactivation of Basp1 attenuates diet-induced NASH in mice; macrophages lacking Basp1 show diminished response to pro-inflammatory stimuli, impaired NLRP3 inflammasome activation, and reduced cytokine secretion, identifying BASP1 as a critical regulator of myeloid inflammatory signaling. Myeloid-specific Basp1 knockout mice, diet-induced NASH model, bulk and single-cell RNA-seq, inflammasome activation assays, cytokine measurements Hepatology (Baltimore, Md.) High 37505219
2008 Human BASP1 is present in the nucleus of HeLa cells under normal conditions; upon caspase activation during apoptosis, BASP1 relocates from the nucleus to the cytoplasm. Novel monoclonal antibody (9B1) identified by LC/MS/MS, immunostaining of apoptotic cells, caspase-dependent labeling analysis Biochemical and biophysical research communications Medium 18457665
2023 Loss of BASP1 in glioma cells results in removal of TRIM37/EZH2 complex-mediated repressive histone modifications (H2A-ub, H3K27me3) and addition of WDR5/MLL complex-mediated active modifications (H3K4me3, H3K9ac) on the FBXO32 promoter, upregulating FBXO32 and activating NF-κB/MGMT signaling via IκBα ubiquitin-dependent degradation. ChIP for histone modifications and chromatin remodeling complexes, Co-IP of TRIM37/EZH2 and WDR5/MLL, siRNA knockdown, MGMT reporter assays, in vitro and in vivo TMZ resistance models Molecular cancer research : MCR Medium 36961398
2026 BASP1 interacts with β-catenin and binds to the MYC promoter to suppress MYC transcription; BASP1 suppresses TNIK protein expression and thereby reduces TCF7L2 phosphorylation required for MYC transcriptional activation; BASP1 suppresses multiple key proteins of the canonical WNT signaling pathway in colorectal cancer cells. Co-IP (BASP1 with β-catenin), ChIP at MYC promoter, proteome and transcriptome analysis, CRISPR-based BASP1 reactivation, TNIK inhibitor experiments Proceedings of the National Academy of Sciences of the United States of America Medium 41785318

Source papers

Stage 0 corpus · 100 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2000 GAP43, MARCKS, and CAP23 modulate PI(4,5)P(2) at plasmalemmal rafts, and regulate cell cortex actin dynamics through a common mechanism. The Journal of cell biology 509 10871285
2000 Shared and unique roles of CAP23 and GAP43 in actin regulation, neurite outgrowth, and anatomical plasticity. The Journal of cell biology 227 10871284
2020 GAP-43 and BASP1 in Axon Regeneration: Implications for the Treatment of Neurodegenerative Diseases. Frontiers in cell and developmental biology 138 33015061
2004 BASP1 is a transcriptional cosuppressor for the Wilms' tumor suppressor protein WT1. Molecular and cellular biology 114 14701728
2005 Nerve ending "signal" proteins GAP-43, MARCKS, and BASP1. International review of cytology 99 16125549
2002 Transcriptional upregulation of SCG10 and CAP-23 is correlated with regeneration of the axons of peripheral and central neurons in vivo. Molecular and cellular neurosciences 98 12213442
1999 Cholesterol-dependent localization of NAP-22 on a neuronal membrane microdomain (raft). The Journal of biological chemistry 89 10409698
2004 Crystal structure of a myristoylated CAP-23/NAP-22 N-terminal domain complexed with Ca2+/calmodulin. The EMBO journal 87 14765114
2009 Inhibition of Myc-induced cell transformation by brain acid-soluble protein 1 (BASP1). Proceedings of the National Academy of Sciences of the United States of America 85 19297618
2010 BASP1 promotes apoptosis in diabetic nephropathy. Journal of the American Society of Nephrology : JASN 82 20110383
1997 The motility-associated proteins GAP-43, MARCKS, and CAP-23 share unique targeting and surface activity-inducing properties. Experimental cell research 76 9344590
2008 Characterization of BASP1-mediated neurite outgrowth. Journal of neuroscience research 70 18438920
1990 Identification, localization, and primary structure of CAP-23, a particle-bound cytosolic protein of early development. The Journal of cell biology 69 2148567
2012 Repression of transcription by WT1-BASP1 requires the myristoylation of BASP1 and the PIP2-dependent recruitment of histone deacetylase. Cell reports 65 22939983
2008 Dynamic interaction between WT1 and BASP1 in transcriptional regulation during differentiation. Nucleic acids research 65 19050011
1997 The BASP1 family of myristoylated proteins abundant in axonal termini. Primary structure analysis and physico-chemical properties. Biochimie 62 9310187
1999 Identification of the calmodulin-binding domain of neuron-specific protein kinase C substrate protein CAP-22/NAP-22. Direct involvement of protein myristoylation in calmodulin-target protein interaction. The Journal of biological chemistry 58 10207003
1994 Inhibitory effect of calmodulin on phosphorylation of NAP-22 with protein kinase C. The Journal of biological chemistry 55 8034714
1997 Identification of NAP-22 and GAP-43 (neuromodulin) as major protein components in a Triton insoluble low density fraction of rat brain. Biochimica et biophysica acta 52 9030206
2008 Identification of novel aberrant methylation of BASP1 and SRD5A2 for early diagnosis of hepatocellular carcinoma by genome-wide search. International journal of oncology 47 18949357
2003 Binding of NAP-22, a calmodulin-binding neuronal protein, to raft-like domains in model membranes. Biochemistry 40 12718518
2011 WT1 and its transcriptional cofactor BASP1 redirect the differentiation pathway of an established blood cell line. The Biochemical journal 36 21269271
2021 LncRNA BASP1-AS1 interacts with YBX1 to regulate Notch transcription and drives the malignancy of melanoma. Cancer science 35 34533860
2004 Cholesterol-dependent partitioning of PtdIns(4,5)P2 into membrane domains by the N-terminal fragment of NAP-22 (neuronal axonal myristoylated membrane protein of 22 kDa). The Biochemical journal 35 14989697
1999 Immunohistochemical localization of a novel acidic calmodulin-binding protein, NAP-22, in the rat brain. Neuroscience 35 10391449
2015 Albumin-induced apoptosis of tubular cells is modulated by BASP1. Cell death & disease 34 25675304
2020 Targeting positive feedback between BASP1 and EGFR as a therapeutic strategy for lung cancer progression. Theranostics 32 33042262
2021 Podocyte apoptosis in diabetic nephropathy by BASP1 activation of the p53 pathway via WT1. Acta physiologica (Oxford, England) 31 33615732
2002 Lipid binding activity of a neuron-specific protein NAP-22 studied in vivo and in vitro. Journal of neuroscience research 31 12271466
2018 Methylation-associated silencing of BASP1 contributes to leukemogenesis in t(8;21) acute myeloid leukemia. Experimental & molecular medicine 30 29674693
2013 Prohibitin is required for transcriptional repression by the WT1-BASP1 complex. Oncogene 29 24166496
2020 LINC00473 inhibits vascular smooth muscle cell viability to promote aneurysm formation via miR-212-5p/BASP1 axis. European journal of pharmacology 28 31954705
2017 BASP1 interacts with oestrogen receptor α and modifies the tamoxifen response. Cell death & disease 27 28492543
1997 Biochemical evidence for the presence of NAP-22, a novel acidic calmodulin binding protein, in the synaptic vesicles of rat brain. Neuroscience letters 26 9086473
2010 Ion channel activity of brain abundant protein BASP1 in planar lipid bilayers. The FEBS journal 24 21156029
1994 Expression and myristoylation of NAP-22 using a baculovirus transfer vector system. Biochimica et biophysica acta 24 8193160
2020 The brain acid-soluble protein 1 (BASP1) interferes with the oncogenic capacity of MYC and its binding to calmodulin. Molecular oncology 23 31944520
2000 The binding of myristoylated N-terminal nonapeptide from neuro-specific protein CAP-23/NAP-22 to calmodulin does not induce the globular structure observed for the calmodulin-nonmyristylated peptide complex. Protein science : a publication of the Protein Society 22 11106163
2021 Cholesterol is required for transcriptional repression by BASP1. Proceedings of the National Academy of Sciences of the United States of America 21 34266955
2006 Tracking peptide-membrane interactions: insights from in situ coupled confocal-atomic force microscopy imaging of NAP-22 peptide insertion and assembly. Journal of structural biology 21 16889981
2003 Natural N-terminal fragments of brain abundant myristoylated protein BASP1. Biochimica et biophysica acta 21 12829256
2020 BASP1 Suppresses Cell Growth and Metastasis through Inhibiting Wnt/β-Catenin Pathway in Gastric Cancer. BioMed research international 20 33426068
2016 High-order oligomers of intrinsically disordered brain proteins BASP1 and GAP-43 preserve the structural disorder. The FEBS journal 20 26918762
2010 The assessment of methylated BASP1 and SRD5A2 levels in the detection of early hepatocellular carcinoma. International journal of oncology 20 19956849
2003 The arrangement of cholesterol in membranes and binding of NAP-22. Chemistry and physics of lipids 20 12598036
2009 Biochemical interaction of an actin-capping protein, CapZ, with NAP-22. Journal of neuroscience research 18 19267422
2005 Induction of raft-like domains by a myristoylated NAP-22 peptide and its Tyr mutant. The FEBS journal 18 15794765
2021 Truncated YY1 interacts with BASP1 through a 339KLK341 motif in YY1 and suppresses vascular smooth muscle cell growth and intimal hyperplasia after vascular injury. Cardiovascular research 17 33508088
2020 WT1 activates transcription of the splice factor kinase SRPK1 gene in PC3 and K562 cancer cells in the absence of corepressor BASP1. Biochimica et biophysica acta. Gene regulatory mechanisms 17 33017668
2009 Subcellular and regional location of "brain" proteins BASP1 and MARCKS in kidney and testis. Acta histochemica 15 19683798
2008 Novel antibody to human BASP1 labels apoptotic cells post-caspase activation. Biochemical and biophysical research communications 15 18457665
2021 BASP1 labels neural stem cells in the neurogenic niches of mammalian brain. Scientific reports 14 33692421
2011 Inhibitory effect of NAP-22 on the phosphatase activity of synaptojanin-1. Journal of neuroscience research 14 21932368
2000 Changes in the localization of NAP-22, a calmodulin binding membrane protein, during the development of neuronal polarity. Neuroscience research 14 10958980
2019 The WT1-BASP1 complex is required to maintain the differentiated state of taste receptor cells. Life science alliance 13 31167803
2013 Interaction of NAP-22 with brain glutamic acid decarboxylase (GAD). Neuroscience letters 12 23376695
2023 Myeloid-specific ablation of Basp1 ameliorates diet-induced NASH in mice by attenuating pro-inflammatory signaling. Hepatology (Baltimore, Md.) 11 37505219
2022 The BASP1 transcriptional corepressor modifies chromatin through lipid-dependent and lipid-independent mechanisms. iScience 11 35982799
2011 Immunoelectron microscopic study of BASP1 and MARCKS location in the early and late rat spermatids. Acta histochemica 11 21764106
2003 Quaternary structure of the neuronal protein NAP-22 in aqueous solution. Biochimica et biophysica acta 11 12922169
2021 Identification of Basp1 as a novel angiogenesis-regulating gene by multi-model system studies. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 10 33899275
2004 Motor, sensory and autonomic nerve terminals containing NAP-22 immunoreactivity in the rat muscle. Brain research 10 14988044
2023 BASP1 promotes high glucose-induced endothelial apoptosis in diabetes via activation of EGFR signaling. Journal of diabetes investigation 9 36756695
2015 Ganglioside contained in the neuronal tissue-enriched acidic protein of 22 kDa (NAP-22) fraction prepared from the detergent-resistant membrane microdomain of rat brain inhibits the phosphatase activity of calcineurin. Journal of neuroscience research 9 25981177
2012 ¹H, ¹³C and ¹⁵N resonance assignments of human BASP1. Biomolecular NMR assignments 9 23179057
2008 BASP1 in the lens. Journal of cellular biochemistry 9 18655186
2003 Specificity of membrane binding of the neuronal protein NAP-22. The Journal of membrane biology 9 12962277
2023 Circ_0008285 silencing suppresses angiotensin II-induced vascular smooth muscle cell apoptosis in thoracic aortic aneurysm via miR-150-5p/BASP1 axis. Thoracic cancer 8 37337843
1998 Characterization of bovine and human cDNAs encoding NAP-22 (22 kDa neuronal tissue-enriched acidic protein) homologs. Molecules and cells 8 9749536
2023 Downregulation of BASP1 Promotes Temozolomide Resistance in Gliomas via Epigenetic Activation of the FBXO32/NF-κB/MGMT Axis. Molecular cancer research : MCR 7 36961398
2023 Dihydroartemisinin inhibits EMT of glioma via gene BASP1 in extrachromosomal DNA. Biochemical and biophysical research communications 7 37473527
2022 LINC00599 influences smoke-related chronic obstructive pulmonary disease and regulates CSE-induced epithelial cell apoptosis and inflammation by targeting miR-212-5p/BASP1 axis. Human & experimental toxicology 7 36541900
2021 The actin-cytoskeleton associating protein BASP1 regulates neural progenitor localization in the neural tube. Genesis (New York, N.Y. : 2000) 7 34897971
2004 Localization of the Cl(-)-ATPase activity on NAP-22 enriched membrane microdomain (raft) of rat brain. Neuroscience letters 7 15193776
1999 Immunohistochemical demonstration of a neuronal calmodulin-binding protein, NAP-22, in the rat spinal cord. Brain research 7 10407094
2015 Tight binding of NAP-22 with acidic membrane lipids. Neuroscience letters 6 26101831
2014 Sequestration of the abrin A chain to the nucleus by BASP1 increases the resistance of cells to abrin toxicity. The Biochemical journal 6 24350992
2008 Morphological analysis on the distribution of membrane lipids and a membrane protein, NAP-22, during neuronal development in vitro. Journal of molecular histology 6 18521709
2025 WTAP-mediated m6A modification on BASP1 mRNA contributes to ferroptosis in AAA. General thoracic and cardiovascular surgery 5 39969669
2018 Interaction of dynamin I with NAP-22, a neuronal protein enriched in the presynaptic region. Neuroscience letters 5 29604406
2025 From inflammation to remodelling: A novel BASP1+ monocyte subset as a catalyst for acute aortic dissection. Journal of advanced research 4 40057028
2023 BASP1 down-regulates RANKL-induced osteoclastogenesis. Experimental cell research 4 37619639
2013 BASP1 and its N-end fragments (BNEMFs) dynamics in rat brain during development. Neurochemical research 4 23579388
2025 Design of lipid-based formulations for oral delivery of a BASP1 peptide targeting MYC-dependent gastrointestinal cancer cells. Journal of controlled release : official journal of the Controlled Release Society 3 40185335
2009 Mutational screening of BASP1 and transcribed processed pseudogene TPPsig-BASP1 in patients with Möbius syndrome. Journal of genetics and genomics = Yi chuan xue bao 3 19376485
2025 LncRNA BASP1-AS1 drives PCBP2 K115 lactylation to suppress ferroptosis and confer oxaliplatin resistance in gastric cancer. Free radical biology & medicine 2 40914325
2024 LncRNA BASP1-AS1 is a positive regulator of stemness and pluripotency in human SH-SY5Y neuroblastoma cells. Biochemical and biophysical research communications 2 39303525
2023 BASP1 knockdown suppresses chondrocyte apoptosis and extracellular matrix degradation in vivo and in vitro: A possible therapeutic approach for osteoarthritis. Experimental cell research 2 37207971
2020 The effects of phospholipids and fatty acids on the oligomer formation of NAP-22. Neuroscience letters 2 32750402
2026 Reactivation of the silenced BASP1 gene suppresses oncogenic WNT signaling in human colorectal cancer cells. Proceedings of the National Academy of Sciences of the United States of America 1 41785318
2025 BASP1/HTRA2 axis, targeted by miR-7a-5p, exerted a pro-apoptosis role in myocardial ischemia/reperfusion injury. Toxicology and applied pharmacology 1 40484205
2025 Membrane binding and clustering of NAP-22, a neuron-enriched intrinsically disordered protein. Biophysical journal 1 41163390
2024 Oligomerization and aggregation of NAP-22 with several metal ions. Neuroscience letters 1 38184017
2013 [Amyloid-like oligomers of presynaptic protein BASP1]. Rossiiskii fiziologicheskii zhurnal imeni I.M. Sechenova 1 25470949
2008 Effect of exogenous calcium deficit on blood pressure and modification of brain proteins GAP-43 and BASP1 in SHR and WKY rats. Bulletin of experimental biology and medicine 1 19039922
1996 [Specific properties and primary structure of BASP1 protein, initially detected in neuronal axonal terminals]. Biokhimiia (Moscow, Russia) 1 9035734
2026 Brain Acid-Soluble Protein 1 (BASP1) maintains germinal centers by regulating germinal center B cell survival. Journal of immunology (Baltimore, Md. : 1950) 0 41171696
2026 LncRNA SNHG14 Participates in the Development of Chronic Obstructive Pulmonary Disease by Targeting the miR-150-5p/BASP1 Axis. Journal of biochemical and molecular toxicology 0 42041191
2025 m6A-Modified BASP1 Regulates IL6 Expression to Induce TAM Infiltration to Promote Gastric Cancer Progression. Journal of gastroenterology and hepatology 0 41251296
2025 BASP1, targeted by miR-185-5p, promotes atherosclerosis via VSMC proliferation and inflammation. American journal of translational research 0 41415108