| 2002 |
p80 CRMP-1 (a novel splice variant of CRMP-1 with an extended N-terminus) was co-immunoprecipitated with ROKα from brain extracts, interacted with the kinase domain of ROKα, and inhibited ROKα catalytic activity toward other substrates. p80 CRMP-1 also formed oligomeric complexes with CRMP-2. Co-overexpression of p80 CRMP-1 and CRMP-2 counteracted RhoA-induced neurite retraction, an effect enhanced by mutation of the ROK phosphorylation site in CRMP-2. |
Co-immunoprecipitation from brain extracts, peptide mass analysis, kinase activity assay, overexpression in neurons |
FEBS letters |
Medium |
12482610
|
| 2005 |
CRMP1 localizes predominantly to dendrites of specific adult neuronal populations (cortical pyramidal neurons, hippocampal CA1 pyramidal cells, Purkinje cells) in adult mouse brain, as determined by immunohistochemistry with specific antibodies. In cultures of cortical neurons CRMP1 is distributed throughout cell bodies, axons, and dendrites. |
Immunohistochemistry with specific antibodies on adult mouse brain sections and primary neuron cultures |
The Journal of comparative neurology |
Medium |
15834957
|
| 2006 |
CRMP1 is required for normal granule cell migration, proliferation, and apoptosis during postnatal cerebellar development. CRMP1-/- mice showed reduced granule cell migration from cerebellar explants, and anti-CRMP1 antibody treatment of wild-type explants replicated this defect. |
CRMP1 knockout mice (knock-in LacZ), cerebellar explant migration assay, antibody blockade, in vivo histology |
Genes to cells : devoted to molecular & cellular mechanisms |
High |
17121542
|
| 2006 |
CRMP-1 was identified as a binding partner of GNE (UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase), the key enzyme of sialic acid biosynthesis, via yeast two-hybrid screening followed by co-immunoprecipitation verification. |
Yeast two-hybrid assay, co-immunoprecipitation |
FEBS letters |
Low |
17118363
|
| 2008 |
NF-κB p50 (but not the classic p65/p50 heterodimer) binds to a κB site in the CRMP-1 promoter region (between -1753 and -1743) and negatively regulates CRMP-1 expression, thereby promoting cancer cell invasion. Antisense p50 increased CRMP-1 protein level and decreased invasiveness. |
EMSA, supershift assay, ChIP, antisense p50 transfection, invasion assay |
Biochemical and biophysical research communications |
Medium |
18782567
|
| 2008 |
Transcription of CRMP-1 is reciprocally regulated at its promoter by C/EBPα (activator) and Sp1 (repressor) competing for overlapping binding sites (-122 to -133 and -101 to -113). COX-2 overexpression decreases CRMP-1 expression by promoting Sp1 binding; COX-2 inhibitor celecoxib increases CRMP-1 expression by reducing Sp1-DNA complex formation and enhancing C/EBPα binding. |
Serial deletion, site-directed mutagenesis, EMSA, antibody supershift, ChIP, luciferase reporter, overexpression |
Molecular cancer therapeutics |
Medium |
18524846
|
| 2011 |
CRMP-1 associates with LCRMP-1 (long isoform of CRMP-1) and disrupts the interaction between LCRMP-1 and WAVE-1, thereby inhibiting LCRMP-1-mediated filopodia formation, actin stabilization, and cancer cell invasion. LCRMP-1 acts downstream of Cdc42 in the WAVE-1/actin nucleation pathway, and CRMP-1 antagonizes this pathway by competing for LCRMP-1 binding. |
Co-immunoprecipitation, overexpression in noninvasive cell lines, filopodia/invasion assays, WAVE-1 interaction assays |
The Journal of clinical investigation |
Medium |
21747164
|
| 2012 |
CRMP1 was identified as insoluble/misfolded protein in post-mortem schizophrenia brains and shown to directly and functionally interact with DISC1 (Disrupted-in-schizophrenia 1), placing CRMP1 at the intersection of reelin and DISC1 pathways. |
Antibodies against pooled insoluble proteome, biochemical fractionation of post-mortem brains, functional interaction assay with DISC1 |
Human molecular genetics |
Low |
22798627
|
| 2012 |
Local inactivation of CRMP1 (by micro-CALI) in the central domain of the growth cone caused lamellipodial retraction and subsequent retardation of neurite outgrowth, whereas inactivation in the neurite shaft arrested neurite outgrowth. Focal inactivation of CRMP1 in one half of the growth cone caused the growth cone to turn away from the irradiated site. These effects were distinct from those of CRMP2 inactivation. |
Microscale chromophore-assisted light inactivation (micro-CALI) with spatial and temporal resolution in live neurons |
Developmental neurobiology |
High |
22378692
|
| 2012 |
CRMP1 and CRMP2 have synergistic roles in Sema3A-dependent dendritic spine maturation. crmp1-/- mice showed reduced dendritic spine density in cortical layer V pyramidal neurons comparable to sema3A-/- and crmp2-/- mice. CRMP1 levels increased in crmp2-/- mice, but there was no genetic interaction between crmp1 and crmp2 on spine density (double heterozygous sema3A+/-;crmp1+/- showed reduced spine density and branching). |
CRMP2 and CRMP1 knockout mice, dendritic spine density quantification, genetic epistasis analysis |
Genes to cells : devoted to molecular & cellular mechanisms |
High |
27480924
|
| 2014 |
CRMP1 binds both the actin-binding domain and the last immunoglobulin-like repeat (rod 24) of Filamin-A. Phosphorylation-mimicking CRMP1(Ser522Asp) enhances Sema3A repulsion in neurons and causes Filamin-A to adopt a condensed form (shown by atomic-force microscopy). Phospho-CRMP1(Ser522Asp) weakens F-actin gelation crosslinked by Filamin-A, suggesting phosphorylated CRMP1 displaces Filamin-A from the actin cytoskeleton to facilitate remodeling. Alanine mutants in the interacting residues of either Filamin-A or CRMP1 suppress Sema3A repulsion. The C. elegans homologue UNC-33 (CRMP1) interacts with FLN-1 (Filamin-A orthologue) and participates in motor neuron projection. |
Pulldown, co-immunoprecipitation, atomic-force microscopy, alanine mutagenesis, F-actin gelation assay, C. elegans genetics |
Nature communications |
High |
25358863
|
| 2014 |
CRMP1 interacts with Speedy A1 (Spy1), a member of the Speedy/RINGO family, as identified by yeast two-hybrid and verified by co-immunoprecipitation. Spy1 modulates CDK5-mediated phosphorylation of CRMP1. Enhanced CRMP1 phosphorylation (promoted by Spy1) disturbs the association of CRMP1 with actin, contributing to abnormal Sema3A-induced growth cone collapse and impaired regeneration after sciatic nerve crush. |
Yeast two-hybrid, co-immunoprecipitation, overexpression/shRNA knockdown, phosphorylation assay, rat sciatic nerve crush model |
Molecular neurobiology |
Medium |
25526860
|
| 2015 |
CRMP1 directly interacts with N-terminal huntingtin (HTT) fragments containing expanded polyglutamine tracts and suppresses their spontaneous self-assembly into proteotoxic aggregates, reducing HTT misfolding and neurotoxicity in multiple HD models. |
Protein-protein interaction network filtering, experimental validation of CRMP1-HTT interaction in HD models (cell and in vivo) |
Genome research |
Medium |
25908449
|
| 2016 |
CRMP1 suppresses EMT and metastasis in prostate cancer cells by associating with actin and WAVE1 (an Arp2/3 activator). CRMP1 knockdown stabilizes F-actin and triggers stress fiber formation; overexpression inhibits EMT and in vivo metastasis. CRMP1 expression is suppressed by histone deacetylation and direct promoter repression by the EMT regulator Snail. |
Co-immunoprecipitation (CRMP1-actin and CRMP1-WAVE1), siRNA knockdown, stable overexpression, F-actin staining, in vivo metastasis assay, ChIP for Snail binding to CRMP1 promoter |
Oncogene |
Medium |
27321179
|
| 2016 |
CRMP1 and CRMP4 redundantly regulate proper orientation of basal dendrites of layer V pyramidal neurons and apical dendrite bifurcation of hippocampal CA1 neurons. CRMP1/CRMP4 double knockout showed severe dendritic orientation abnormalities not seen in single knockouts. |
CRMP1 and CRMP4 single and double knockout mice, cortical and hippocampal neuron morphology analysis |
Brain research |
Medium |
27836492
|
| 2017 |
CRMP1 functionally couples with Nav1.7 (SCN9A) to mediate Sema3A-induced retrograde axonal transport of PlexA4 and TrkA from growth cones. In crmp1-/- DRG neurons, Sema3A-induced co-localization and retrograde transport of PlexA4 and TrkA were impaired (similar to Nav1.7 RNAi knockdown). Sema3A induced co-localization of CRMP1 and Nav1.7 in growth cones. Introduction of CRMP1 in HEK293 cells lowered the activation threshold of co-expressed Nav1.7. |
crmp1-/- mouse DRG neurons, RNAi knockdown of Nav1.7, immunofluorescence co-localization, electrophysiology in HEK293 cells |
Journal of cell science |
High |
28254884
|
| 2021 |
Fyn kinase phosphorylates CRMP1 at Tyrosine 504 (Tyr504), and this phosphorylation is required for Sema3A-induced growth cone collapse and dendritic development. CRMP1-Tyr504Phe mutant suppressed Sema3A-induced growth cone collapse in DRG and hippocampal neurons and impaired cortical dendritic development in vivo. Fyn+/-;Crmp1+/- double heterozygous mice showed poor basal dendrite development similar to Sema3a-/-, Fyn-/-, and Crmp1-/- mice. |
In vitro kinase assay (Fyn phosphorylating CRMP1 Tyr504), site-directed mutagenesis (Tyr504Phe), growth cone collapse assay, in vivo cortical neuron morphology, double heterozygous genetic epistasis |
Journal of neurochemistry |
High |
33449368
|
| 2021 |
FEZ1 interacts with CRMP1 at neuronal growth cones. FEZ1 deficiency in hippocampal neurons caused growth cone collapse and impaired axonal development phenotypically similar to CRMP1 loss-of-function, placing FEZ1 upstream or in the same pathway as CRMP1 in growth cone guidance. |
Co-immunoprecipitation, immunofluorescence co-localization, FEZ1 knockdown with morphological readout, comparison to CRMP1 loss-of-function |
eNeuro |
Medium |
33771901
|
| 2022 |
Inhibition of CRMP1 phosphorylation at Ser522 (using Crmp1S522A knock-in mice) improved motor function and preserved motor neurons and neuromuscular junctions in SOD1G93A ALS model mice, whereas CRMP1 knockout worsened outcomes. Phospho-mimicking CRMP1 mutant overexpression inhibited axonal outgrowth in Neuro2A cells. Phosphorylated CRMP1 (pCRMP1) accumulates in spheroids in ALS patient spinal cords and co-localizes with phosphorylated neurofilaments. |
Crmp1 Ser522Ala knock-in and CRMP1 KO mice in SOD1G93A background, rotarod test, motor neuron/NMJ histology, phosphoproteomic identification, phospho-mimicking mutant overexpression, human ALS patient immunostaining |
eNeuro / Frontiers in neurology |
High |
35523582 36237616
|
| 2022 |
De novo heterozygous variants in CRMP1 impair CRMP1 oligomerization and suppress neurite outgrowth in murine cortical neurons upon overexpression, linking CRMP1 oligomerization to its role in neurite development. |
In silico structural analysis, oligomerization assay, neurite outgrowth assay in primary cortical neurons with overexpression of variants |
eLife |
Medium |
36511780
|
| 2022 |
CRMP1 and CRMP2 redundantly regulate migration and positioning of Purkinje cells in cerebellar lobule X. CRMP1/CRMP2 double knockout mice showed deficits in Purkinje cell migration and alignment in lobule X and impaired performance on the balance beam test. |
CRMP1/CRMP2 double knockout mice, cerebellar histology, balance beam and grip power tests |
Brain research |
Medium |
35219721
|
| 2022 |
CRMP1 is expressed in cochlear outer and inner hair cells, and its deletion causes progressive high-frequency hearing loss and hair cell loss at the basal cochlear region without affecting hair cell morphogenesis. |
Immunostaining, Crmp1 knockout mice, scanning electron microscopy, auditory brainstem response testing |
The American journal of pathology |
Medium |
35181334
|
| 2023 |
LKB1 physically interacts with CRMP1 (co-immunoprecipitation) in regenerated sciatic nerve axons, and LKB1 regulates CRMP1 phosphorylation. Overexpression of both LKB1 and CRMP1 promotes Schwann cell invasion/migration and neuronal process extension; knockdown of CRMP1 abolishes LKB1's nerve repair-promoting function. |
Co-immunoprecipitation, immunofluorescence co-localization, overexpression and siRNA knockdown, Schwann cell invasion assay, rat sciatic nerve crush model |
Developmental neurobiology |
Medium |
38105470
|
| 2023 |
Deletion of CRMP1 in mice disrupts the balance between synaptic and extrasynaptic NMDA receptors in the hippocampus, increasing extrasynaptic NMDA receptor levels and tau phosphorylation, leading to synaptic and neuronal loss in CA3 and accelerated age-related cognitive decline. |
crmp1 KO mice at adult/middle-aged/older stages, Morris water maze, biochemical fractionation for synaptic/extrasynaptic NMDA receptor levels, glutamate/glutamine measurement |
Neurobiology of aging |
Medium |
38176125
|