| 1989 |
The microtubule-binding domain of MAP1B was mapped to a highly basic region containing repeated KKEE/KKEVI motifs; this region copurifies with microtubules in vitro and mediates microtubule interaction in vivo in transfected cells. A separate 12-repeat region does not bind microtubules. The MAP1B microtubule-binding domain is structurally unrelated to those of MAP2, tau, or kinesin. |
Cell-free translation of subcloned fragments + microtubule cosedimentation cycles in vitro; full-length and deletion constructs transfected into cultured cells with immunofluorescence readout |
The Journal of Cell Biology |
High |
2480963
|
| 1991 |
MAP1B is encoded as a polyprotein: the heavy chain and light chain 1 (LC1) are translated from the same mRNA within the same open reading frame and generated by proteolytic processing. LC1 binds near the heavy-chain N-terminus and together they form a complex microtubule-binding domain. |
Amino acid sequencing of heavy-chain fragment, epitope mapping, Northern and Southern blotting; co-purification of heavy chain and LC1 |
Neuron |
High |
1712602
|
| 1994 |
Light chain 3 (LC3) is a subunit of both MAP1A and MAP1B complexes; purified recombinant LC3 associates with microtubules assembled in the presence of brain MAPs and with microtubules assembled from purified tubulin, demonstrating a direct microtubule-binding activity. |
cDNA sequencing, microtubule cosedimentation assays with recombinant LC3, immunoprecipitation, Western blot |
The Journal of Biological Chemistry |
High |
7908909
|
| 1988 |
MAP1B is phosphorylated in vitro by a casein kinase II (CK2)-like activity present in developing neuroblastoma cells; phosphopeptide maps of brain MAP1B phosphorylated by purified CK2 are identical to those of in vivo phosphorylated neuroblastoma MAP1B, identifying CK2 as a principal kinase acting on MAP1B during neurite outgrowth. |
In vitro kinase assay with purified CK2 and other kinases; phosphopeptide mapping; immunoprecipitation; microtubule cosedimentation |
The Journal of Cell Biology |
High |
3164313
|
| 1992 |
Expression of MAP1B in fibroblasts stabilizes microtubules against depolymerizing reagents and increases alpha-tubulin acetylation, demonstrating that MAP1B promotes microtubule stability in vivo, though without the extensive microtubule bundling induced by MAP2 or tau. |
cDNA transfection into COS/HeLa/3T3 cells; nocodazole resistance assay; immunofluorescence for acetylated tubulin |
Journal of Cell Science |
High |
1487506
|
| 1998 |
The MAP1B light chain (LC1), in the absence of the heavy chain, induces formation of nocodazole- and taxol-resistant stable microtubules; the heavy chain inhibits LC1 activity. LC1 contains a C-terminal actin filament-binding domain, and LC1 can dimerize/oligomerize. Heavy chain–light chain interaction domains were localized by coimmunoprecipitation of epitope-tagged fragments. |
Transient transfection in COS cells; immunofluorescence; nocodazole/taxol resistance assay; coimmunoprecipitation of epitope-tagged fragments; actin cosedimentation |
The Journal of Cell Biology |
High |
9813091
|
| 1999 |
MAP1B specifically interacts with the GABA(C) receptor rho1 subunit (but not GABA(A) subunits), co-localizes with GABA(C) receptors at bipolar cell axon terminals in the retina, and redistributes rho1 upon co-expression in COS cells, suggesting MAP1B anchors GABA(C) receptors at postsynaptic sites. |
Yeast two-hybrid (interaction discovery), co-immunoprecipitation, immunofluorescence co-localization in retinal slices, heterologous co-expression redistribution assay in COS cells |
Nature |
High |
9892354
|
| 2000 |
Twelve amino acids at the C-terminus of the large intracellular loop of rho1 (and rho2) are sufficient for interaction with MAP1B; disrupting the MAP1B–rho1 interaction in bipolar cells in retinal slices decreased the EC50 of GABA(C) receptors, doubling current at low GABA concentrations without affecting maximum current, demonstrating that cytoskeletal anchoring by MAP1B modulates GABA(C) receptor sensitivity. |
Deletion/mutagenesis mapping of rho1 interaction domain; patch-clamp electrophysiology of retinal bipolar cells in slices after disruption of MAP1B–rho interaction |
The Journal of Neuroscience |
High |
11102469
|
| 1998 |
GSK-3β directly phosphorylates MAP1B in vitro; in cerebellar granule neurons, WNT-7a and lithium (a GSK-3β inhibitor) induce loss of the phosphorylated form of MAP1B (MAP1B-P) from axonal processes before axonal remodelling is visible, identifying MAP1B as a downstream target of the WNT–GSK-3β pathway in axonal remodelling. |
In vitro phosphorylation assay with purified GSK-3β and MAP1B; immunostaining of granule neurons treated with lithium or WNT-7a; time-course imaging of axonal morphology |
Journal of Cell Science |
High |
9570753
|
| 2005 |
GSK-3β phosphorylates MAP1B at Ser1260 and Thr1265 in vitro and in vivo; phospho-specific antibodies show that GSK-3β-phosphorylated MAP1B is restricted to growing axons (distal gradient) in developing rat embryos. Site-directed mutation (Ser1260Val or Thr1265Val, or both) in full-length MAP1B alters microtubule dynamics in transfected cells, establishing these sites as a molecular switch regulating microtubule stability in growing axons. |
Site-directed mutagenesis of recombinant MAP1B; in vitro GSK-3β kinase assay; phospho-specific antibody generation; immunostaining of developing nervous system; heterologous cell transfection with MT dynamics assay |
Journal of Cell Science |
High |
15731007
|
| 2005 |
Gigaxonin (GAN protein) binds MAP1B light chain (LC) through its C-terminal kelch repeat domain; gigaxonin overexpression leads to enhanced proteasome-dependent degradation of MAP1B-LC; GAN-null neurons accumulate MAP1B-LC; MAP1B overexpression causes neuronal death similar to GAN-null neurons, while MAP1B knockdown improves GAN-null neuron survival, identifying gigaxonin as a ubiquitin scaffolding protein controlling MAP1B-LC degradation and neuronal survival. |
Pull-down, co-immunoprecipitation; overexpression in neurons; proteasome inhibitor experiments; GAN knockout mouse neurons; MAP1B siRNA knockdown; cell viability assay |
Nature |
High |
16227972
|
| 2000 |
MAP1B null mice (complete null allele) are viable but selectively lack the corpus callosum due to misguided cortical axons, and have reduced/thinner myelinated axons in peripheral nerves with decreased nerve conduction velocity, demonstrating an essential role for MAP1B in axon guidance and CNS/PNS development. |
Gene targeting (complete null allele), histology, electrophysiological nerve conduction velocity measurement, immunohistochemistry |
The Journal of Cell Biology |
High |
11121433
|
| 2000 |
Tau and MAP1B cooperate synergistically in axonal elongation and neuronal migration: double-knockout (tau−/−map1b−/−) mice show much more severe defects (inhibited axonal elongation in hippocampal neurons, delayed neuronal migration in cerebellar neurons) than single knockouts, demonstrating functional redundancy between the two MAPs. |
Double-knockout mouse generation; primary hippocampal and cerebellar neuron cultures from knockout mice; morphological analysis of axon elongation and migration |
The Journal of Cell Biology |
High |
10973990
|
| 2004 |
Netrin-1 regulates mode I MAP1B phosphorylation (activating GSK-3 and CDK5) both in vivo and in vitro; MAP1B-deficient neurons show reduced chemoattractive response to Netrin-1 in vitro, and map1b mutant mice display severe axonal tract abnormalities similar to netrin-1-deficient mice, placing MAP1B as a downstream effector in Netrin-1 signaling for axon guidance and neuronal migration. |
In vitro phosphorylation assays; Netrin-1 treatment of wild-type and map1b-null neurons; chemoattraction assay; analysis of map1b and netrin-1 mutant mouse brain anatomy |
Current Biology |
High |
15186740
|
| 2004 |
Reelin induces mode I MAP1B phosphorylation through GSK-3 and CDK5 activation, with mDab1 participating in the signaling cascade; map1b-deficient mice have abnormal cortical layering consistent with a failure of neuronal migration, placing MAP1B downstream of Reelin signaling. |
In vitro and in vivo phosphorylation assays after Reelin treatment; analysis of map1b-null mouse brain lamination; mDab1 involvement tested biochemically |
Cerebral Cortex |
Medium |
15590913
|
| 2005 |
The MAPK pathway (not the PI3K pathway) links NGF/TrkA receptor engagement to GSK-3β activation, which then phosphorylates MAP1B to regulate microtubule dynamics and axon growth rate; pharmacological inhibition of MAPK prevents GSK-3β activation and MAP1B phosphorylation and reduces neurite growth, while PI3K inhibition does not. |
Pharmacological inhibitor studies (MAPK and PI3K inhibitors) in PC12 cells and sympathetic neurons; in vitro kinase assay; GSK-3β activation assay |
Molecular and Cellular Neurosciences |
Medium |
15737742
|
| 2003 |
NGF activates GSK-3β phosphorylation of MAP1B through TrkA receptors, not through p75NTR; BDNF (which activates p75NTR but not TrkA) does not stimulate this phosphorylation; TrkA-deficient PC12 nnr cells fail to show NGF-dependent MAP1B phosphorylation; TrkA inhibition blocks neurite elongation and MAP1B phosphorylation. |
Use of receptor-selective ligands and PC12 nnr cells lacking TrkA; TrkA kinase inhibitor (K252a); in vivo immunostaining for phospho-MAP1B |
Journal of Neurochemistry |
Medium |
14622124
|
| 2008 |
DAPK-1 (death-associated protein kinase 1) binds directly to the N-terminal domain of MAP1B (residues 1–126 and a 12-aa motif); amino acid starvation induces a stable endogenous MAP1B–DAPK-1 immune complex; MAP1B is required for DAPK-1-stimulated autophagy and membrane blebbing: MAP1B siRNA attenuates these DAPK-1 activities, and MAP1B overexpression synergizes with DAPK-1 for growth inhibition. |
Peptide library selection; immunobinding assays; confocal co-localization; siRNA knockdown; clonogenic growth assay; autophagy and blebbing phenotype assays |
The Journal of Biological Chemistry |
Medium |
18195017
|
| 2009 |
DYRK1A acts as a priming kinase for GSK-3β phosphorylation of MAP1B; mass spectrometry identified 28 MAP1B phosphorylation sites; DYRK1A-primed GSK-3β sites are distributed throughout the neuron while non-primed GSK-3β sites are restricted to growing axons; DYRK1A knockdown compromises neuritogenesis and alters microtubule stability. |
Mass spectrometry phosphosite mapping; phospho-specific antibody panel; kinase inhibitor treatments in embryonic cortical neurons; shRNA knockdown of DYRK1A; EB3 microtubule dynamics imaging |
Journal of Cell Science |
High |
19549690
|
| 1993 |
Protein phosphatase 2A (PP2A) and PP2B (calcineurin) dephosphorylate mode I (proline-directed) MAP1B phosphorylation sites, while mode II (CK2-type) sites are dephosphorylated by PP2A and PP1 but not PP2B; inhibition of PP2A in rat brain slices (okadaic acid) increases MAP1B phosphorylation and inhibits its microtubule-binding activity. |
In vitro phosphatase assay with purified PP1, PP2A, PP2B; phosphorylation-state antibodies on rat brain slices treated with okadaic acid or cyclosporin A; microtubule binding assay |
FEBS Letters |
Medium |
7690334
|
| 2000 |
PP2A is the major phosphatase regulating MAP1B phosphorylation and microtubule-binding activity in rat brain: okadaic acid (PP2A inhibitor) treatment of brain slices markedly increases MAP1B phosphorylation and inhibits MAP1B microtubule-binding activity; cyclosporin A (PP2B inhibitor) has a lesser effect. |
Okadaic acid and cyclosporin A treatment of metabolically active rat brain slices; Western blot with phospho-MAP1B antibodies; immunocytochemistry; microtubule binding assay |
Brain Research |
Medium |
10640627
|
| 1996 |
Dephosphorylated MAP1B (but not native phosphorylated MAP1B) binds and cosediments with microfilaments in vitro; the proline-directed kinase (PDPK) phosphorylation site (not the CK2 sites) negatively regulates MAP1B interaction with F-actin. |
In vitro alkaline phosphatase dephosphorylation; F-actin cosedimentation assay; dephosphorylation kinetics correlated with F-actin binding |
FEBS Letters |
Medium |
8690071
|
| 2002 |
MAP1B light chain 1 (LC1) binds microtubules and induces tubulin polymerization via a critical NH2-terminal microtubule-binding domain; LC1 also contains a C-terminal actin-binding domain that directly binds actin filaments; the two MAP1 light chains (LC1 of MAP1B and LC2 of MAP1A) differ in their effects on microtubule bundling and stability despite structural similarity. |
In vivo microtubule/actin binding assays in transfected cells; in vitro tubulin polymerization assay; domain deletion analysis; immunofluorescence |
The Journal of Neuroscience |
Medium |
11896150
|
| 2007 |
MAP1B heavy chain directly binds actin; co-immunoprecipitation shows actin and tubulin co-precipitate with MAP1B at similar ratios throughout development regardless of phosphorylation state; atomic force microscopy measures MAP1B–actin binding force comparable to MAP1B–tubulin interaction. MAP1B heavy chain thus contains both a microtubule-stabilizing domain and an actin-binding site. |
Co-immunoprecipitation from brain tissue; mass spectrometry identification; atomic force microscopy force measurement; electron microscopy; COS-7 cell immunofluorescence |
Brain Research Bulletin |
Medium |
17292804
|
| 2010 |
MAP1B deficiency reduces Rac1 and Cdc42 activity and increases RhoA activity; MAP1B interacts with Tiam1 (a Rac1 GEF); constitutively active Rac1, Cdc42, or Tiam1 rescues axon growth defects in MAP1B-deficient neurons, establishing a MAP1B–Tiam1–Rac1 axis required for microtubule–actin crosstalk during neuronal polarization. |
MAP1B-null mouse neurons; Rac1/Cdc42/RhoA activity pull-down assays; co-immunoprecipitation of MAP1B with Tiam1; rescue by constitutively active GTPase constructs; axon outgrowth assay |
Molecular Biology of the Cell |
High |
20719958
|
| 2011 |
MAP1B is present in dendritic spines; MAP1B-deficient mice show decreased density of mature dendritic spines, increased filopodia-like protrusions, reduced AMPA receptor-mediated synaptic currents, decreased Rac1 activity, increased RhoA activity, and decreased phospho-cofilin in postsynaptic densities, implicating MAP1B in dendritic spine maturation via actin cytoskeleton regulation. |
MAP1B+/- mouse neurons; spine morphology analysis; patch-clamp electrophysiology; Rac1/RhoA activity assays; Western blot of PSD fractions |
The Journal of Biological Chemistry |
High |
21984824
|
| 2013 |
MAP1B interacts directly with EB1 and EB3 (+TIP proteins) and sequesters them in the neuronal cytosol; MAP1B overexpression reduces EB binding to microtubule plus-ends, while MAP1B knockdown increases EB-MT association and causes microtubule overstabilization and looping in growth cones, resulting in delayed axon outgrowth. |
Co-immunoprecipitation; direct interaction assay; RNAi knockdown; EB3-GFP live imaging of microtubule dynamics; growth cone morphology analysis |
The EMBO Journal |
High |
23572079
|
| 2011 |
MAP1B knockdown in embryonic rat cortical neurons decreases microtubule growth speed in the proximal and distal axon shaft (but not in growth cone filopodia) and produces more branched, slower growing axons; expression of MAP1B in MAP1B-naive cells increases microtubule elongation rate, demonstrating that MAP1B enhances microtubule assembly rates. |
RNAi knockdown; EB3-GFP live imaging of microtubule polymerization speed; axon morphology analysis; MAP1B expression in heterologous cells |
Molecular and Cellular Neurosciences |
High |
22033417
|
| 2013 |
MAP1B deficiency impairs LTD expression specifically by preventing AMPA receptor endocytosis and spine shrinkage during LTD; this is due to failure of Tiam1 (Rac1 GEF) targeting to synaptic compartments and reduced Rac1 activation; providing additional Rac1 restores LTD and AMPA receptor endocytosis in MAP1B-deficient neurons, establishing a MAP1B–Tiam1–Rac1 relay for synaptic plasticity. |
Conditional MAP1B-deficient mouse + shRNA; electrophysiological LTD recording; AMPA receptor endocytosis assay; Tiam1 localization by immunostaining; Rac1 activity assay; rescue with Rac1 expression |
The EMBO Journal |
High |
23881099
|
| 2012 |
Dystonin-a2 binds MAP1B in the centrosomal region; loss of this interaction in dt mutant neurons causes altered MAP1B perikaryal localization, microtubule deacetylation and instability, Golgi fragmentation, and impaired anterograde trafficking; restoring MT acetylation (trichostatin A) or MAP1B overexpression rescues these defects. |
Dystonin mutant mouse + isoform-specific RNAi; co-immunoprecipitation; immunofluorescence of MAP1B and acetylated tubulin; Golgi morphology; vesicle trafficking assay; rescue experiments |
The Journal of Cell Biology |
High |
22412020
|
| 2012 |
S-nitrosylation of MAP1B light chain 1 (LC1) induces a conformational change that activates LC1 and promotes its ubiquitination by MITOL (mitochondrial ubiquitin ligase); MITOL inhibition results in accumulation of S-nitrosylated LC1, mitochondrial dysfunction, and neuronal cell death, demonstrating that MITOL regulates MAP1B-LC1 through nitrosylation-dependent ubiquitination. |
S-nitrosylation assay; MITOL knockdown/overexpression; ubiquitination assay; mitochondrial function assay; neuronal cell death readout; conformational change analysis |
Proceedings of the National Academy of Sciences USA |
High |
22308378
|
| 2012 |
Syk protein-tyrosine kinase uses MAP1B as a major substrate to promote microtubule stability in MDA-MB-231 breast cancer cells; MAP1B silencing attenuates Syk-dependent microtubule acetylation and nocodazole resistance, and reverses Syk-induced changes in cell topography/stiffness measured by atomic force microscopy. |
Syk expression/silencing; MAP1B siRNA; nocodazole resistance assay; acetylated tubulin immunostaining; multiharmonic AFM nanomechanical mapping |
Biochemistry |
Medium |
24914616
|
| 2012 |
Nav1.6 (SCN8A) voltage-gated sodium channel N-terminus interacts with MAP1B light chain via residues 77–80 (VAVP) of Nav1.6; co-expression of Nav1.6 with Map1b in ND7/23 neuronal cells increases sodium current density 50%; mutation of the Map1b-binding site of Nav1.6 prevents generation of sodium current, demonstrating that MAP1B facilitates Nav1.6 trafficking to the neuronal cell surface. |
Yeast two-hybrid screen; co-immunoprecipitation from mouse brain; alanine-scanning mutagenesis; patch-clamp electrophysiology in transfected cells |
The Journal of Biological Chemistry |
High |
22474336
|
| 2009 |
Nemo-like kinase (NLK) directly phosphorylates MAP1B in vitro; NGF promotes NLK translocation to leading edges of PC12 cells and activates NLK kinase activity; NLK knockdown reduces MAP1B phosphorylation and inhibits NGF-induced F-actin redistribution and neurite outgrowth. |
In vitro kinase assay with purified NLK and MAP1B; NLK knockdown; immunofluorescence of F-actin and NLK; neurite outgrowth assay |
Journal of Neurochemistry |
Medium |
19840224
|
| 2006 |
QKI RNA-binding protein binds the 3'UTR of MAP1B mRNA in oligodendroglia; QKI-deficiency (quakingviable mice) reduces MAP1B mRNA expression; QKI knockdown destabilizes MAP1B mRNA in CG4 cells; forced QKI expression is sufficient to promote MAP1B expression, demonstrating QKI-dependent mRNA stabilization as a post-transcriptional mechanism controlling MAP1B levels specifically in oligodendroglia. |
3'UTR binding assay; qv mutant mice analysis; RNAi knockdown of QKI; QKI overexpression; Northern blot / qPCR for MAP1B mRNA stability |
Molecular Biology of the Cell |
Medium |
16855020
|
| 2011 |
Staufen 2 (Stau2) knockdown reduces dendritic localization of Map1b mRNA, decreases basal Map1b protein in dendrites, and prevents mGluR/DHPG-induced increases in dendritic Map1b protein; Stau2 is required for mGluR-LTD (but not LTP); mGluR stimulation induces Map1b mRNA dissociation from Stau2/P0-containing granules, demonstrating Stau2 controls Map1b mRNA dendritic distribution and translation for mGluR-LTD. |
Stau2 shRNA knockdown; Map1b mRNA FISH; protein immunostaining in dendrites; electrophysiology (LTP, LTD); granule co-localization; DHPG stimulation |
Learning & Memory |
Medium |
21508097
|
| 2012 |
In growth cones, a DLK–MKK7–JNK1 MAP kinase module phosphorylates Map1b to regulate microtubule bundling and neurite elongation; MKK7 mRNA localizes to the growth cone and can be locally translated there; disruption of this pathway alters Map1b phosphorylation and microtubule bundling. |
Genome-wide mRNA localization screen; MKK7 mRNA FISH in growth cones; phospho-Map1b immunostaining; kinase inhibitor and dominant-negative experiments; neurite elongation assay |
PLoS Biology |
Medium |
23226105
|
| 2007 |
MAP1B coordinates microtubule and actin cytoskeleton remodeling; MAP1B is required for LPA-induced microtubule backfolding during process retraction in DRG neurons and Schwann cells; MAP1B-deficient cells show actin contraction but fail to execute the subsequent microtubule backfolding step, and MAP1B is required for Schwann cell migration in vitro. |
Map1b-null mouse neurons and Schwann cells; LPA stimulation; time-lapse imaging of cytoskeletal rearrangements; migration assay |
Molecular and Cellular Neurosciences |
Medium |
17764972
|
| 2016 |
GSK-3-mediated MAP1B phosphorylation is locally reduced at neurite branching points; MAP1B is required downstream of GSK-3 for branching control, as map1b−/− neurons are not affected by GSK-3 inhibition and re-expression of MAP1B in map1b−/− neurons restores wild-type branching. Phospho-MAP1B preferentially associates with tyrosinated microtubules and its dephosphorylation by GSK-3 inhibition protects both tyrosinated and acetylated MTs from nocodazole depolymerization. |
Map1b-null mouse neurons; GSK-3 inhibitor treatments; cDNA rescue transfection; MAP1B-transfected fibroblasts + nocodazole assay; phospho-MAP1B immunostaining at branch points; tyrosinated/acetylated tubulin staining |
Molecular and Cellular Neurosciences |
Medium |
26773468
|
| 2015 |
FMRP associates with miR-181d, Map1b mRNA, and Calm1 mRNA in axons; miR-181d delivered by FMRP negatively regulates local translation of MAP1B in axons; FMRP deficiency (Fmr1I304N or Fmr1 knockdown) impedes axonal delivery of miR-181d and Map1b mRNA, reducing MAP1B protein in axons; NGF releases Map1b mRNA from FMRP/miR-181d-repressing granules to promote axon elongation. |
FMRP co-immunoprecipitation with miR-181d and Map1b mRNA; microfluidic axon isolation; MAP1B protein quantification in axons; NGF stimulation; Fmr1 mutant mice |
Cell Reports |
Medium |
26711345
|
| 2019 |
In SNCA-A53T (Parkinson's disease) human neurons, mutant α-synuclein fails to complex with PKC, impairing Nrf2 activation; reduced Nrf2 activity on antioxidant response elements (AREs) at the Map1b gene enhancer decreases MAP1B expression; forced MAP1B expression or Nrf2 activation rescues neuritic length/complexity defects in PD neurons. |
hPSC-derived A9-type dopaminergic neurons + isogenic controls; ChIP-seq/reporter assay for Nrf2 on Map1b ARE; MAP1B overexpression rescue; Nrf2 pharmaceutical activation; neuritic morphology analysis |
Proceedings of the National Academy of Sciences USA |
Medium |
31235589
|
| 2016 |
MAP1B-deficient neurons show decreased density of presynaptic terminals, increased proportion of orphan presynaptic terminals, altered synaptic vesicle fusion (FM4-64 assay), and decreased density of synaptic vesicles and dense core vesicles at presynaptic terminals, identifying a presynaptic structural and functional role for MAP1B. |
MAP1B KO mouse neurons; immunofluorescence quantification of synaptic terminal density; FM4-64 synaptic vesicle fusion assay; electron microscopy of presynaptic terminals |
Scientific Reports |
Medium |
27425640
|
| 2020 |
MAP1B mutations (c.4198A>G p.S1400G; c.2768T>C p.I923T; c.5512T>C p.F1838L) cause reduced MAP1B levels and deficient MAP1B phosphorylation in patient-derived otic sensory neuron-like cells; these cells exhibit disturbed microtubule dynamics, impaired axonal elongation, and electrophysiological defects, all rescued by CRISPR/Cas9 correction of the MAP1B mutation; Map1b+/- mice show progressive hearing loss with spiral ganglion neuron microtubule phosphorylation defects. |
Patient iPSC-derived otic neurons; CRISPR/Cas9 correction; Map1b+/- mouse audiometry; MAP1B phosphorylation Western blot; microtubule dynamics imaging; patch-clamp electrophysiology |
JCI Insight |
High |
33268592
|