Affinage

MAP1A

Microtubule-associated protein 1A · UniProt P78559

Length
2803 aa
Mass
305.5 kDa
Annotated
2026-06-10
45 papers in source corpus 25 papers cited in narrative 25 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

MAP1A is a large, filamentous neuronal microtubule-associated protein that assembles as a multi-subunit complex of a heavy chain and light chains (LC2, LC3) to nucleate, elongate, stabilize, and crosslink microtubules and to physically couple them to the actin cytoskeleton (PMID:3553448, PMID:7918469, PMID:11896150). Purified native MAP1A drives both nucleation and elongation of tubulin polymerization, lowers the critical concentration for assembly, and binds 13–15 tubulin dimers per molecule (PMID:7918469); it engages microtubules through an unusual acidic, repeat-free microtubule-binding domain sufficient for autonomous binding and microtubule stabilization (PMID:8006079), and efficient filamentous decoration of microtubules requires the joint action of the heavy chain and LC2 (PMID:15936015). Beyond tubulin, MAP1A and its LC2 subunit bind and crosslink F-actin via a distinct C-terminal actin-binding domain, establishing LC2 as a linker between microtubule and microfilament networks (PMID:7820861, PMID:11896150); the LC3 subunit independently suppresses microtubule dynamics (PMID:19233279). The light chains also serve as protein-interaction hubs: LC2 binds the PSD-95 guanylate kinase domain through a phosphorylation-independent interaction in which a conserved MAP1A aspartate mimics a phosphoserine (PMID:17220895, PMID:28701415), and recruits signaling proteins including EPAC1/EPAC2 (potentiating cAMP-stimulated Rap1 activation) (PMID:15202935, PMID:15591041), GTP-loaded RhoB (regulating EGF receptor expression) (PMID:18056259), the presynaptic Cav2.2 calcium channel (anchoring it to the actin cytoskeleton to maintain surface expression and Ca2+ influx) (PMID:18971475), and DISC1 (PMID:12812986), while CK1δ binds and phosphorylates LC2 (PMID:15961172). In vivo, loss of MAP1A causes Purkinje cell degeneration with dendritic swellings, disrupted axon initial segment and somatodendritic microtubule networks, and reduced PSD-93 (PMID:25788676). In disease contexts MAP1A is a degradative and post-translational target: Aβ oligomers trigger its caspase-3/calpain-dependent proteolysis (PMID:16234245), and α-synuclein fibril–induced nitrosative stress drives MAP1A S-nitrosylation upstream of NMDAR dysfunction (PMID:36414406).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 1984 High

    Established that MAP1A is a bona fide microtubule-associated protein in living cells, anchoring all later mechanistic work to the cytoskeleton.

    Evidence Immunofluorescence with monoclonal antibody, tubulin co-localization, and colchicine/vinblastine/taxol perturbation across 18 mammalian cell lines

    PMID:6142895

    Open questions at the time
    • Did not define the molecular binding domain
    • No information on subunit composition or stoichiometry
  2. 1987 High

    Resolved MAP1A's physical form, showing it is a long flexible filament that builds cross-bridges between dendritic microtubules rather than a compact globular MAP.

    Evidence Immunoelectron microscopy, quick-freeze deep-etch, and rotary shadowing in Purkinje cell dendrites

    PMID:3553448

    Open questions at the time
    • Crosslinking partners beyond microtubules not defined
    • Molecular basis of cross-bridge formation unknown
  3. 1994 High

    Defined MAP1A's biochemical activity on tubulin and identified an atypical acidic microtubule-binding domain, explaining how MAP1A stabilizes microtubules distinctly from MAP2/tau.

    Evidence Turbidimetric assembly kinetics and stoichiometry with purified native MAP1A; cDNA expression constructs with nocodazole-resistance assays

    PMID:7918469 PMID:8006079

    Open questions at the time
    • Structural basis of acidic-domain microtubule contact not determined
    • Regulation of binding activity in vivo unknown
  4. 1994 High

    Showed MAP1A also binds and crosslinks actin and that LC3 is a shared microtubule-binding subunit, introducing the dual-cytoskeletal-linker and modular-light-chain themes.

    Evidence F-actin co-sedimentation, viscometry, and solid-phase immunoassay with purified MAP1A; recombinant LC3 microtubule co-sedimentation

    PMID:7820861 PMID:7908909

    Open questions at the time
    • Whether actin and microtubule binding are simultaneous not established
    • LC3 contribution within the holo-complex not quantified
  5. 2002 High

    Localized the dual-cytoskeleton linker activity to LC2, mapping separable N-terminal microtubule-binding and C-terminal actin-binding domains.

    Evidence In vitro and in vivo microtubule binding, tubulin polymerization, deletion mutagenesis, and actin co-sedimentation

    PMID:11896150

    Open questions at the time
    • Whether LC2 simultaneously bridges both filament types in cells unresolved
    • Functional consequence of bridging for neuronal architecture not yet tested
  6. 2007 Medium

    Reconstituted the minimal MAP1A complex requirement, demonstrating heavy chain and LC2 must co-assemble for efficient filamentous microtubule decoration.

    Evidence Tagged-construct transfection in COS7/Neuro2A, nocodazole-resistance assays, and yeast two-hybrid (reported 2005)

    PMID:15936015

    Open questions at the time
    • Stoichiometry of the assembled complex not defined
    • In vitro reconstitution of heavy chain/LC2 binding not performed
  7. 2008 Medium

    Established MAP1A LC2 as a scaffold beyond the cytoskeleton, defining structurally and biochemically resolved interactions with PSD-95 GK, EPAC1/2, CK1δ, RhoB, and DISC1.

    Evidence Yeast/mammalian two-hybrid, co-IP, GST pulldown, NMR, in vitro kinase, Rap1 GTPase, and EGFR signaling assays across multiple studies

    PMID:12812986 PMID:15202935 PMID:15591041 PMID:15961172 PMID:17220895 PMID:18056259

    Open questions at the time
    • Most interactions rest on single-lab assays
    • How simultaneous scaffolding is coordinated on one LC2 molecule unknown
  8. 2008 High

    Demonstrated a physiological scaffolding role at synapses, showing LC2 anchors Cav2.2 channels to the actin cytoskeleton to maintain presynaptic surface expression and calcium influx.

    Evidence Co-IP, surface-epitope detection, RNAi, Ca2+ imaging, FM4-64 uptake, Latrunculin A treatment, and actin-binding-domain truncation rescue

    PMID:18971475

    Open questions at the time
    • Whether the holo-MAP1A complex or free LC2 mediates anchoring unclear
    • Generalizability to other channels not tested
  9. 2009 Medium

    Differentiated the light chains functionally, showing LC3 suppresses microtubule dynamics without conferring nocodazole resistance whereas LC1/LC2 form resistant bundles.

    Evidence Live-cell microtubule dynamics measurement, in vitro binding, and nocodazole-resistance assays

    PMID:19233279

    Open questions at the time
    • Mechanistic basis of differing light-chain effects unresolved
    • Behavior within the native MAP1A complex not addressed
  10. 2015 High

    Provided in vivo loss-of-function evidence that MAP1A is required for neuronal microtubule network integrity and survival, linking the protein to Purkinje cell degeneration and PSD-93 maintenance.

    Evidence Spontaneous and targeted mouse knockouts with immunofluorescence, histology, and immunoblotting

    PMID:25788676

    Open questions at the time
    • Whether MAP1B redistribution drives or compensates for the phenotype unclear
    • Causal link between PSD-93 loss and degeneration not dissected
  11. 2022 Medium

    Placed MAP1A within neurodegenerative pathways as a degradative and post-translational target, with Aβ-driven proteolysis and α-synuclein–driven S-nitrosylation upstream of NMDAR dysfunction.

    Evidence Caspase-3/calpain inhibitor and antioxidant assays in primary neurons (2005); calcium imaging and NOS inhibition with α-syn preformed fibrils (2022)

    PMID:16234245 PMID:36414406

    Open questions at the time
    • S-nitrosylation site on MAP1A not mapped
    • Mechanistic link from modified MAP1A to NMDAR remains correlative
  12. 2024 Medium

    Extended MAP1A's cytoskeletal-organizer role beyond neurons, showing it coordinates microtubule, actin, vimentin, and septin networks in Sertoli cells via a p38-MAPK pathway.

    Evidence RNAi knockdown, immunofluorescence, RNA-Seq, cadmium injury model, and doramapimod rescue

    PMID:38570783

    Open questions at the time
    • Direct MAP1A interaction with non-tubulin cytoskeletal elements not shown
    • How p38-MAPK couples to MAP1A disruption unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the full MAP1A heavy chain/light chain holo-complex integrates simultaneous microtubule crosslinking, actin coupling, and multivalent signaling scaffolding into a single regulated unit remains unresolved.
  • No structure of the assembled heavy chain/light chain complex
  • Phospho-regulation by CK1δ not linked to specific functional outputs in vivo
  • Whether scaffolding interactions occur on holo-complex or free light chains untested

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0008092 cytoskeletal protein binding 5 GO:0060090 molecular adaptor activity 4 GO:0005198 structural molecule activity 2
Localization
GO:0005856 cytoskeleton 4
Pathway
R-HSA-112316 Neuronal System 3 R-HSA-162582 Signal Transduction 2
Partners
CACNA1BCSNK1DDISC1EPAC1MAP1BPSD-95RHOBSNTA1
Complex memberships
MAP1A heavy chain/light chain complex

Evidence

Reading pass · 25 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1994 MAP1A light chain 3 (LC3) is a microtubule-binding subunit of both MAP1A and MAP1B; purified recombinant LC3 associates with microtubules assembled in the presence of brain MAPs and with microtubules assembled from purified tubulin, indicating LC3 functions as a MAP1A/MAP1B subunit that can regulate their microtubule-binding activity. cDNA sequencing, in vitro microtubule co-sedimentation assay with purified recombinant LC3 The Journal of biological chemistry High 7908909
1984 MAP1A localizes along microtubules (mitotic spindle and interphase cytoplasmic fibers) in a wide variety of mammalian cell types; co-localization with tubulin, disappearance upon colchicine/vinblastine treatment, and reorganization by taxol confirmed microtubule association. The punctate staining pattern suggests MAP1A contacts microtubules at discrete foci. Immunofluorescence microscopy with monoclonal antibody, co-localization with tubulin, drug-treatment experiments (colchicine, vinblastine, taxol), immunoblot analysis The Journal of cell biology High 6142895
1987 MAP1A forms filamentous cross-bridges between microtubules in Purkinje cell dendrites; immunoelectron microscopy showed gold particles on filamentous materials connected to microtubules but not to neurofilaments; rotary shadowing revealed MAP1A is a long, thin, flexible filamentous molecule. Immunoelectron microscopy with monoclonal antibody and gold-labeled secondary antibody; quick-freeze deep-etch; rotary shadowing The Journal of neuroscience High 3553448
1994 MAP1A binds to both G-actin and F-actin, crosslinks F-actin (causing gelation and increased viscosity), and co-sediments with the gelled actin network; MAP1A and MAP2 bind to common or overlapping sites on actin. Solid-phase immunoassay, F-actin co-sedimentation, viscometry, SDS-PAGE analysis of purified native MAP1A Cell motility and the cytoskeleton High 7820861
1994 A novel microtubule-binding domain in MAP1A was identified that is rich in charged amino acids, is acidic (unlike all other known mammalian microtubule-binding domains which are basic), lacks sequence repeats, and is sufficient for autonomous microtubule binding. Expression of this domain stabilized microtubules against nocodazole and produced a distinct rearrangement pattern compared to MAP2 or tau. cDNA expression constructs transfected into cultured cell lines, co-localization with microtubules, nocodazole resistance assay Journal of cell science Medium 8006079
1994 Purified native MAP1A promotes both nucleation and elongation of tubulin polymerization, binds 13–15 mol of tubulin dimers per MAP1A molecule, lowers the critical concentration for assembly, and has higher kinetic rate constants (K+1 and K-1) than MAP2. Turbidimetry-based microtubule assembly kinetics, ion-exchange purification, stoichiometry analysis with purified MAP1A Biochemistry High 7918469
2002 MAP1A light chain 2 (LC2) binds to microtubules in vivo and in vitro, induces rapid tubulin polymerization via an N-terminal microtubule-binding domain, and also contains a C-terminal actin filament-binding domain that directly interacts with actin. LC2 differs from LC1 (MAP1B light chain) in its effects on microtubule bundling and stability in vivo, establishing LC2 as a potential linker between neuronal microtubules and microfilaments. In vitro microtubule binding assays, in vivo localization, tubulin polymerization assays, deletion mutagenesis, actin co-sedimentation The Journal of neuroscience High 11896150
2003 DISC1 interacts with MAP1A via the LC2 domain of MAP1A binding to the N-terminus of DISC1, as determined by yeast two-hybrid, mammalian two-hybrid, and co-immunoprecipitation assays. Yeast two-hybrid, mammalian two-hybrid, co-immunoprecipitation, deletion mapping Human molecular genetics Medium 12812986
2004 Caldendrin (a neuronal Ca2+-sensor protein) specifically binds to light chain 3 (LC3) of MAP1A/MAP1B at two binding sites; one site shows strict Ca2+-dependency while both require the first two EF-hands of caldendrin. Calmodulin, despite high sequence similarity to caldendrin, cannot bind LC3 at either site. Yeast two-hybrid, biochemical interaction assays, Ca2+-dependency experiments, deletion/mutagenesis analysis, computer modelling Journal of molecular biology Medium 15095872
2004 LC2 of MAP1A interacts with the cAMP-binding domain of EPAC1 (exchange protein directly activated by cAMP 1); deletion of the cAMP-binding domain of EPAC1 abolished LC2 interaction in two-hybrid assay; LC2 was found to interact with a GST-fusion of the cAMP-binding domain but not DEP, REM, or CAT domains; EPAC2 also co-immunoprecipitated with LC2 from rat cerebellum. Yeast two-hybrid screen, co-immunoprecipitation, GST pulldown assay, immunolocalization The Biochemical journal Medium 15202935
2004 LC2 enhances both basal and cAMP-stimulated Rap1 GTPase activation by EPAC1; LC2 elicits conformational changes in the cAMP-binding domain of EPAC1 increasing its sensitivity to cAMP activation; disruption of endogenous EPAC1/LC2 interaction abolished Rap1 activity in PC12 cells; LC2/EPAC1 co-expression enhanced cell adhesion to laminin. Part of LC2's enhancement of EPAC1 activity is through microtubule stabilization (nocodazole partially blocked the effect). Simultaneous expression system, Rap1 GTPase activation assays, cyclic AMP-agarose binding assay, antibody-mediated disruption of endogenous interaction, cell adhesion assay, nocodazole treatment The Journal of biological chemistry Medium 15591041
2005 Casein kinase 1 delta (CK1δ) interacts with a 176-aa fragment of MAP1A LC2 (LC2-P16) at two interaction domains in LC2 (near aa 2629–2753 and 2712–2805), and LC2 is phosphorylated by CK1δ as a substrate, suggesting CK1δ modulates microtubule dynamics by changing the phosphorylation status of LC2. Yeast two-hybrid, co-immunoprecipitation, in vitro kinase assay, deletion mapping Biochimica et biophysica acta Medium 15961172
2005 Both the MAP1A heavy chain and LC2 are required for efficient microtubule co-localization; neither heavy chain nor LC2 alone produced filamentous structures along microtubules in COS7 cells, but co-expression of both enabled co-localization with microtubules; yeast two-hybrid confirmed the N-terminal heavy chain/LC2 interaction is important for microtubule binding; full MAP1A and LC2 protected microtubules against nocodazole. Transfection of tagged constructs in COS7 and Neuro2A cells, fluorescence microscopy, nocodazole resistance assay, yeast two-hybrid Experimental cell research Medium 15936015
2007 The guanylate kinase (GK) domain of PSD-95 directly binds a conserved motif in MAP1A; structural modeling defined a consensus GK-binding sequence in MAP1A; the GK domain uses its GMP-binding region, which has evolved conformational flexibility allowing it to bind diverse protein partners including MAP1A. Biochemical interaction assays, NMR structural analysis, deletion mutagenesis defining consensus binding sequence Nature structural & molecular biology High 17220895
2007 LC2 of MAP1A interacts with GTP-bound RhoB (GTP-loading and the 18-aa C-terminal hypervariable domain of RhoB are critical for binding); downregulation of MAP1A/LC2 decreased EGF receptor expression and modified EGF signaling responses, placing LC2 as critical for RhoB function in EGF-induced receptor regulation. Yeast two-hybrid screen, GST pulldown assay, co-immunoprecipitation, immunofluorescence, RNAi knockdown, EGF receptor expression analysis The Journal of biological chemistry Medium 18056259
2008 MAP1A LC2 mediates presynaptic surface retention of Cav2.2 calcium channels via a 23-residue binding domain in the Cav2.2 C-terminus; RNAi knockdown of LC2 reduced surface expression of endogenous Cav2.2 at presynaptic boutons, decreased Ca2+-influx into nerve terminals, and impaired activity-dependent FM4-64 uptake; an LC2 truncation lacking the actin-binding domain could not rescue Cav2.2 surface expression, indicating LC2 anchors surface Cav2.2 to the actin cytoskeleton. Co-immunoprecipitation, extracellular epitope antibody to detect surface Cav2.2, RNAi knockdown, Ca2+ imaging, FM4-64 uptake assay, Latrunculin A treatment, rescue experiments with truncation mutant The Journal of neuroscience High 18971475
2009 MAP1A-associated LC3 stabilizes microtubules by decreasing microtubule dynamicity and promoting growth over shortening events (suppression of dynamics), but does not render microtubules resistant to nocodazole-induced depolymerization; in contrast, LC1 and LC2 form nocodazole-resistant bundles. All three light chains co-localize with microtubules and bind taxol-stabilized microtubules in vitro. Fluorescence microscopy, in vitro microtubule binding assay, nocodazole resistance assay, live-cell measurement of microtubule dynamics Molecular and cellular neurosciences Medium 19233279
2005 Soluble Abeta oligomers induce sequential proteolysis of MAP1A and MAP1B through the combined action of caspase-3 and calpain (following Ca2+ homeostasis perturbation); calpain activation alone is sufficient for MAP2 isoform proteolysis but MAP1A and MAP1B proteolysis requires both caspase-3 and calpain activation; antioxidants prevent MAP1A proteolysis, highlighting an upstream role for reactive oxygen species. Time-course degradation assays in primary neurons, caspase-3 and calpain inhibitor treatments, antioxidant rescue, immunoblotting The Journal of biological chemistry Medium 16234245
2012 Osteopontin (OPN) associates with MAP1A and MAP1B in rat substantia nigra and striatum, confirmed by affinity pull-down, co-immunoprecipitation, and immunohistochemistry; site-directed mutagenesis of OPN (Y165A, D139E) inhibited some of these interactions. Yeast two-hybrid, affinity pull-down, co-immunoprecipitation, immunohistochemistry, site-directed mutagenesis The European journal of neuroscience Medium 22779921
2012 The conserved C-terminal ~125-aa domain (located in the light chains of MAP1A, MAP1B, and MAP1S) directly interacts with α1-syntrophin through the PH2 and PDZ domains of α1-syntrophin; the MAP1A/MAP1B light chain–α1-syntrophin interaction was confirmed by yeast two-hybrid and co-immunoprecipitation from mouse brain. Yeast two-hybrid screen, co-immunoprecipitation from mouse brain, co-localization in transfected cells PloS one Medium 23152929
2015 Loss of MAP1A in mice (spontaneous nm2719 mutation and targeted deletion) causes Purkinje cell degeneration with dendritic focal swellings, disruptions in axon initial segment (AIS) morphology, reduction of the microtubule network in somatodendritic and AIS compartments, aberrant redistribution of MAP1B heavy and light chains to soma/dendrites, and reduction of the MAGUK scaffold protein PSD-93 in Purkinje cells. Spontaneous mouse mutation characterization, targeted gene knockout, immunofluorescence, histology, immunoblotting The Journal of neuroscience High 25788676
2017 Crystal structure of PSD-95 GK domain in complex with a MAP1A peptide at 2.6-Å resolution reveals the MAP1A peptide adopts a unique conformation where hydrophobic residues cluster to interact with the 'hydrophobic site' of PSD-95 GK, and a conserved aspartic acid (D2117) of MAP1A mimics phosphoserine/threonine binding to the 'phospho-site'—a phosphorylation-independent interaction distinct from canonical phosphopeptide-GK complexes. X-ray crystallography at 2.6-Å resolution, structural comparison with phosphopeptide complexes The Biochemical journal High 28701415
2022 α-Synuclein preformed fibril-induced accumulation promotes nitric oxide synthesis and S-nitrosylation of MAP1A; inhibition of nitric oxide synthase (with L-NAME) blocked MAP1A S-nitrosylation and normalized NMDAR-dependent calcium transients and overall network activity, placing MAP1A S-nitrosylation downstream of α-syn aggregation-induced nitrosative stress and upstream of NMDAR dysfunction. Live-cell calcium imaging, network activity assays, nitric oxide synthase inhibitor (L-NAME) treatment, S-nitrosylation detection, primary rat cortical neurons with preformed fibrils The Journal of neuroscience Medium 36414406
2024 Map1a knockdown in Sertoli cells disrupts microtubule structural organization and secondarily perturbs actin, vimentin, and septin cytoskeletal organization; cadmium-induced Map1a redistribution is associated with p38-MAPK phosphorylation, and the p38-MAPK inhibitor doramapimod restored MT structural organization after cadmium injury, placing p-p38-MAPK activation in the pathway of cadmium-induced Sertoli cell injury downstream of Map1a disruption. RNAi knockdown, immunofluorescence, RNA-Seq, transcriptome profiling, biochemical cytoskeletal assays, toxicant injury model, pharmacological inhibition with doramapimod Reproductive biology and endocrinology Medium 38570783
1991 Estramustine specifically binds MAP1A in Du145a cells (confirmed by [3H]estramustine drug uptake and fluorography), causing disruption of MAP1A-associated microtubule networks and inhibiting type IV collagenase secretion; pulse-labeling excluded effects on protein synthesis or turnover. Immunofluorescence, immunoprecipitation, [3H]estramustine uptake and fluorography, pulse-labeling Journal of cell science Medium 1647395

Source papers

Stage 0 corpus · 45 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2003 DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation. Human molecular genetics 314 12812986
1994 Molecular characterization of light chain 3. A microtubule binding subunit of MAP1A and MAP1B. The Journal of biological chemistry 239 7908909
1989 Microtubule formation and neurite growth in cerebellar macroneurons which develop in vitro: evidence for the involvement of the microtubule-associated proteins, MAP-1a, HMW-MAP2 and Tau. Brain research. Developmental brain research 149 2509111
1990 Molecular cloning of microtubule-associated protein 1 (MAP1A) and microtubule-associated protein 5 (MAP1B): identification of distinct genes and their differential expression in developing brain. Journal of neurochemistry 137 2355215
1984 Widespread cellular distribution of MAP-1A (microtubule-associated protein 1A) in the mitotic spindle and on interphase microtubules. The Journal of cell biology 104 6142895
2005 Microtubule-associated protein MAP1A, MAP1B, and MAP2 proteolysis during soluble amyloid beta-peptide-induced neuronal apoptosis. Synergistic involvement of calpain and caspase-3. The Journal of biological chemistry 103 16234245
2002 Similar ultrastructural distribution of the 5-HT(2A) serotonin receptor and microtubule-associated protein MAP1A in cortical dendrites of adult rat. Neuroscience 82 12123681
2002 Microtubule-associated protein 1A (MAP1A) and MAP1B: light chains determine distinct functional properties. The Journal of neuroscience : the official journal of the Society for Neuroscience 81 11896150
1987 The molecular structure of microtubule-associated protein 1A (MAP1A) in vivo and in vitro. An immunoelectron microscopy and quick-freeze, deep-etch study. The Journal of neuroscience : the official journal of the Society for Neuroscience 78 3553448
1994 Microtubule associated protein MAP1A is an actin-binding and crosslinking protein. Cell motility and the cytoskeleton 61 7820861
2015 Mutations in the microtubule-associated protein 1A (Map1a) gene cause Purkinje cell degeneration. The Journal of neuroscience : the official journal of the Society for Neuroscience 52 25788676
1996 Gene localization and developmental expression of light chain 3: a common subunit of microtubule-associated protein 1A(MAP1A) and MAP1B. Journal of neuroscience research 48 8833088
2004 Caldendrin but not calmodulin binds to light chain 3 of MAP1A/B: an association with the microtubule cytoskeleton highlighting exclusive binding partners for neuronal Ca(2+)-sensor proteins. Journal of molecular biology 45 15095872
2007 The guanylate kinase domain of the MAGUK PSD-95 binds dynamically to a conserved motif in MAP1a. Nature structural & molecular biology 40 17220895
1994 Identification of a novel microtubule-binding domain in microtubule-associated protein 1A (MAP1A). Journal of cell science 40 8006079
2004 MAP1A light chain 2 interacts with exchange protein activated by cyclic AMP 1 (EPAC1) to enhance Rap1 GTPase activity and cell adhesion. The Journal of biological chemistry 32 15591041
2004 Exchange protein directly activated by cAMP (EPAC) interacts with the light chain (LC) 2 of MAP1A. The Biochemical journal 30 15202935
2005 Interaction of casein kinase 1 delta (CK1 delta) with the light chain LC2 of microtubule associated protein 1A (MAP1A). Biochimica et biophysica acta 29 15961172
2002 Role for RFX transcription factors in non-neuronal cell-specific inactivation of the microtubule-associated protein MAP1A promoter. The Journal of biological chemistry 29 12411430
1996 Human microtubule-associated protein 1a (MAP1A) gene: genomic organization, cDNA sequence, and developmental- and tissue-specific expression. Genomics 29 8812494
1994 Purified native microtubule associated protein MAP1A: kinetics of microtubule assembly and MAP1A/tubulin stoichiometry. Biochemistry 28 7918469
2008 The role of MAP1A light chain 2 in synaptic surface retention of Cav2.2 channels in hippocampal neurons. The Journal of neuroscience : the official journal of the Society for Neuroscience 25 18971475
1987 Differentiation of the cerebellar granule cell: expression of a synaptic vesicle protein and the microtubule-associated protein MAP1A. Brain research 24 3304538
2007 MAP1A light chain-2 interacts with GTP-RhoB to control epidermal growth factor (EGF)-dependent EGF receptor signaling. The Journal of biological chemistry 21 18056259
1993 Sulphonate buffers affect the recovery of microtubule-associated proteins MAP1 and MAP2: evidence that MAP1A promotes microtubule assembly. Cell motility and the cytoskeleton 21 8221901
2012 A yeast two-hybrid screen reveals that osteopontin associates with MAP1A and MAP1B in addition to other proteins linked to microtubule stability, apoptosis and protein degradation in the human brain. The European journal of neuroscience 20 22779921
1996 Differential distribution of MAP1a and aldolase c in adult mouse cerebellum. The European journal of neuroscience 18 8713450
2009 MAP1a associated light chain 3 increases microtubule stability by suppressing microtubule dynamics. Molecular and cellular neurosciences 17 19233279
2005 The functional cooperation of MAP1A heavy chain and light chain 2 in the binding of microtubules. Experimental cell research 13 15936015
2012 The light chains of microtubule-associated proteins MAP1A and MAP1B interact with α1-syntrophin in the central and peripheral nervous system. PloS one 11 23152929
1991 Evidence that estramustine binds MAP-1A to inhibit type IV collagenase secretion. Journal of cell science 10 1647395
2022 Intracellular Accumulation of α-Synuclein Aggregates Promotes S-Nitrosylation of MAP1A Leading to Decreased NMDAR-Evoked Calcium Influx and Loss of Mature Synaptic Spines. The Journal of neuroscience : the official journal of the Society for Neuroscience 8 36414406
2012 The microtubule-associated protein 1A (MAP1A) is an early molecular target of soluble Aβ-peptide. Cellular and molecular neurobiology 8 22252785
1995 Brain-specific expression of human microtubule-associated protein 1A (MAP1A) gene and its assignment to human chromosome 15. Journal of neuroscience research 8 7629894
2024 Map-1a regulates Sertoli cell BTB dynamics through the cytoskeletal organization of microtubule and F-actin. Reproductive biology and endocrinology : RB&E 7 38570783
2003 Distribution of MAP1A, MAP1B, and MAP2A&B during layer formation in the optic tectum of developing chick embryos. Cell and tissue research 7 14523640
2017 Structure of the PSD-95/MAP1A complex reveals a unique target recognition mode of the MAGUK GK domain. The Biochemical journal 6 28701415
2000 Expression of MAP1a and MAP1b in the ganglionic eminence and the internal capsule of the human fetal brain. Neuroscience research 6 11164566
1995 Accumulation of microtubule-associated protein 1A (MAP1A) in differentiating P19 embryonal carcinoma cells. Biochemistry and cell biology = Biochimie et biologie cellulaire 6 8714690
2002 Microtubule associated protein (MAP1A) mRNA was up-regulated by hypergravity in the rat inner ear. Brain research. Molecular brain research 5 12480186
2011 Myotonic dystrophy type 1-associated CTG repeats disturb the expression and subcellular distribution of microtubule-associated proteins MAP1A, MAP2, and MAP6/STOP in PC12 cells. Molecular biology reports 3 21567201
2004 Differential distribution of MAP1A isoforms in the adult mouse barrel cortex and comparison with the serotonin 5-HT2A receptor. Journal of chemical neuroanatomy 3 15121214
1994 Purification of brain microtubule-associated protein MAP1A. Neurochemical research 2 7824074
2026 Serum MAP1A as a Potential Biomarker for Autism Spectrum Disorder. Brain sciences 0 42192792
2025 RNA sequencing identifies MAP1A and PTTG1 as predictive genes of aging CD264+ human mesenchymal stem cells at an early passage. Cytotechnology 0 39980838

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