ArticleThe Journal of biological chemistry2011
Collapsin response mediator proteins (CRMPs) are a new class of microtubule-associated protein (MAP) that selectively interacts with assembled microtubules via a taxol-sensitive binding interaction.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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Who cites it
55 citing papers in PubMed, 98 citations in OpenAlex.
- Changes in Dpysl2 expression are associated with prenatally stressed rat offspring and susceptibility to schizophrenia in humans.International journal of molecular medicine · 2015Trial
- Ketogenic Diet-Associated Remodeling of the Cortical Proteome in Rats With Genetic Absence Epilepsy.Brain and behavior · 2026Article
- Mapping Phosphorylation-Specific Pin1-CRMP2 Interactions Using an Integrated Mass Spectrometry Approach.ACS chemical biology · 2026Article
- Dynamic microtubules as sensors in animal cells.Biophysical journal · 2026Review
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- Contribution of the dihydropyrimidinase-like proteins family in synaptic physiology and in neurodevelopmental disorders.Frontiers in neuroscience · 2023Review
- Cypin binds to tubulin heterodimers and microtubule protofilaments and regulates microtubule spacing in developing hippocampal neurons.Molecular and cellular neurosciences · 2022Article
- Implication of Adipogenesis-Coupled CRMP2 Functional Profile in Metabolic Homeostasis and Imbalance.Biomedicines · 2022Article
- CRMP2 derived from cancer associated fibroblasts facilitates progression of ovarian cancer via HIF-1α-glycolysis signaling pathway.Cell death & disease · 2022Article
- Spastin interacts with collapsin response mediator protein 3 to regulate neurite growth and branching.Neural regeneration research · 2021Article
- DPYSL2 as potential diagnostic and prognostic biomarker linked to immune infiltration in lung adenocarcinoma.World journal of surgical oncology · 2021Article
- Proteomic Analysis Unveils Expressional Changes in Cytoskeleton- and Synaptic Plasticity-Associated Proteins in Rat Brain Six Months after Withdrawal from Morphine.Life (Basel, Switzerland) · 2021Article
- Cortical transcriptome analysis after spinal cord injury reveals the regenerative mechanism of central nervous system in CRMP2 knock-in mice.Neural regeneration research · 2021Article
- CRMP/UNC-33 organizes microtubule bundles for KIF5-mediated mitochondrial distribution to axon.PLoS genetics · 2021Article
- Pyr1-Mediated Pharmacological Inhibition of LIM Kinase Restores Synaptic Plasticity and Normal Behavior in a Mouse Model of Schizophrenia.Frontiers in pharmacology · 2021Article
- Beyond Neuronal Microtubule Stabilization: MAP6 and CRMPS, Two Converging Stories.Frontiers in molecular neuroscience · 2021Article
- GSK3β Interacts With CRMP2 and Notch1 and Controls T-Cell Motility.Frontiers in immunology · 2021Article
- With the Permission of Microtubules: An Updated Overview on Microtubule Function During Axon Pathfinding.Frontiers in molecular neuroscience · 2021Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Collapsin response mediator proteins are ubiquitously expressed from multiple genes (CRMPs 1-5) and play important roles in dividing cells and during semaphorin 3A (Sema3A) signaling. Nonetheless, their mode of action remains opaque. Here we carried out in vivo and in vitro assays that demonstrate that CRMPs are a new class of microtubule-associated protein (MAP). In experiments with CRMP1 or CRMP2 and their derivatives, only the C-terminal region (residues 490-572) mediated microtubule binding. The in vivo microtubule association of CRMPs was abolished by taxol or epothilone B, which is highly unusual. CRMP2-depleted cells exhibited destabilized anaphase astral microtubules and altered spindle position. In a cell-based assay, all CRMPs stabilized interphase microtubules against nocodazole-mediated depolymerization, with CRMP1 being the most potent. Remarkably, a 82-residue C-terminal region of CRMP1 or CRMP2, unrelated to other microtubule binding motifs, is sufficient to stabilize microtubules. In cells, we demonstrate that glycogen synthase kinase-3β (GSK3β) inhibition potentiates this activity. Thus, CRMPs are a new class of MAP that binds through a unique motif, but in common with others such as Tau, is antagonized by GSK3β. This regulation is consistent with such kinases being critical for the Sema3A (collapsin) pathway. These findings have implications for cancer and neurodegeneration.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.