Ask about this productRelated genes to: CLASP2 antibody
- Gene:
- CLASP2 NIH gene
- Name:
- cytoplasmic linker associated protein 2
- Previous symbol:
- -
- Synonyms:
- KIAA0627
- Chromosome:
- 3p22.3
- Locus Type:
- gene with protein product
- Date approved:
- 2002-06-12
- Date modifiied:
- 2016-10-05
Related products to: CLASP2 antibody
Related articles to: CLASP2 antibody
- Microtubules are cytoskeletal polymers that play essential roles in eukaryotic cells, including structural support, cell division, and intracellular transport. During intracellular transport, kinesin motor proteins move cargo along microtubule tracks via their processive stepping. Recent studies have shown that the kinesin-1 KIF5C can damage the microtubule lattice while stepping. Microtubule damage can be repaired through incorporation of new tubulin subunits, however, excessive lattice damage results in microtubule breakage and disassembly. To identify cellular factors involved in microtubule repair, we performed an siRNA screen targeting microtubule-associated proteins (MAPs) known to regulate microtubule dynamics and stability. Based on the results, we investigated whether the end binding protein EB1 and cytoplasmic linker-associated protein 2 (CLASP2) contribute to repair of microtubule damage. To test this, we used a microtubule destruction assay in which damage was induced in microtubules gliding over surfaces coated with wild-type or mutant KIF5C proteins. Our findings suggest that CLASP2 directly facilitates microtubule repair, whereas EB1 does not. We further examined CLASP function using a microtubule repair assay and found that CLASP2 promotes repair by enhancing tubulin incorporation and reducing microtubule breakage. Together, these findings demonstrate that CLASP proteins play an important role in repairing and protecting against lattice damage caused by kinesin-1 motor activity. Our results further suggest that MAPs can directly regulate microtubule lattice integrity under mechanical stress generated by motor protein-driven intracellular transport. - Source: PubMed
Publication date: 2026/06/30
Keya Jakia JannatRiberio RahulYue YangLawrence Elizabeth JZanic MarijaVerhey Kristen J - The manchette is a transient microtubule (MT)-based structure that is vital for the correct shaping of sperm during spermiogenesis. Throughout spermiogenesis, the manchette retains structural integrity for several days, raising the question of how its MTs are regulated. Here, using cryo-electron tomography of manchettes isolated from rat testes, we find that manchette MT ends are structurally diverse. We show that the MT-binding protein CLASP2 is present throughout the manchette and likely regulates both MT ends. Using cryo-electron microscopy single particle analysis and super-resolution microscopy, we reveal that SPACA9 and MNMIP1 (SH3D21) bind to the seam of manchette MTs from the luminal side. SPACA9 binds to both α- and β-tubulin of protofilament 1 but does not interact directly with protofilament 13, while MNMIP1 binds directly to protofilament 13. MNMIP1 further extends and threads through the MT lattice at the seam. Our study reveals a novel seam MT inner protein complex with a unique binding mode, providing a plausible explanation for MT regulation that maintains manchette integrity over an extended period. - Source: PubMed
Publication date: 2026/06/12
Judernatz Jo HDoroshev SvetlanaHoogebeen Robin AJonkers SvenSchweizer DonnaGravett Molly S CBromfield Elizabeth GHowes Stuart CAkhmanova AnnaZhang RuiZeev-Ben-Mordehai Tzviya - Radiotherapy often causes severe and irreversible neural damage, including cognitive impairment and depression-like behaviors. Current mitigants are limited, with single-target molecules being ineffective and nanomedicines posing complexity and toxicity risks. Dragon's Blood (DB), a nontoxic, brown-red resin extracted from (Lour.) (S. C. Chen, China), possesses diverse pharmacological properties. Extensive studies demonstrated that the compounds in DB exhibit multiple therapeutic effects, including cardiovascular protection, promotion of blood circulation, and anti-inflammatory effect. Herein, DB's neuronal radiation mitigation effect and mechanism were investigated. In a whole-brain irradiation rat model, DB administration significantly alleviated radiation-induced anhedonia-like behavior, normalized calcium dyshomeostasis, restored mitochondrial membrane potential, mitigated dendritic spine loss, suppressed neuroinflammation (IL-1β and TNF-α), and preserved hippocampal cytoarchitecture. Brain tissue proteomics revealed 23 DB-modulated KEGG pathways, encompassing the glutamatergic/GABAergic synapse, synaptic plasticity, addiction-related pathways, calcium/cAMP signaling, and hormonal regulation. Ensemble analysis integrating proteomics, WGCNA, machine learning, and PPI pinpointed 24 DB radiation mitigation-related proteins. Among these, eight targets (Grin1, Gabra4, Grm2, Grm3, Grm7, Prkcb, Shank3, and Pak7) functioning via ligand-target interactions were dysregulated by radiation and restored by DB. Molecular docking identified three DB ingredients (socotrin-4'-ol, cinnabarone, and 2'-methoxysocotrin-5'-ol) interacted with all eight targets. Plasma proteomics further revealed radiation mitigation-related brain-enriched proteins (Mib1, Gucy1b1, Fkbp1a, Synj1, and Clasp2). PPI between these 5 plasma proteins and 24 brain proteins reveals DB's multitarget radiation mitigation effect on neurotransmission and synaptic regulation, neuroplasticity, and signaling transduction and cellular response. This work nominated DB and its key constituents as promising candidates for mitigating radiotherapy-induced neural injury. - Source: PubMed
Publication date: 2025/11/25
Li BoyangHan ChuZhang HanLi Bo - Adeno-associated virus (AAV) is a widely used vector for gene delivery, yet the host intracellular trafficking barriers often limit its therapeutic efficacy. Here, we identify microtubule detyrosination - a microtubule post-translational modification - as a key regulator of AAV2 endo-lysosomal processing. Using super-resolution microscopy (SIM/STORM), we show that upon AAV2 endocytosis, the host upregulates microtubule detyrosination via the GSK3β-CLASP2 signaling axis. Single-particle tracking of recombinant virus reveals that detyrosinated microtubules form a physical and functional barrier, restricting AAV2 motility and promoting lysosomal trapping. Restoring microtubule tyrosination via tubulin-tyrosine ligase overexpression or pharmacological inhibition of detyrosination with parthenolide, enhances endosomal escape and perinuclear accumulation of AAV2, translating to improved gene delivery in host cells. Notably, a clinically relevant pro-drug of parthenolide (DMAPT) also displayed a similar trend of enhancing AAV2-driven coagulation factor IX expression in hemophilia B mouse models. Our findings uncover a host mechanism that reshapes the microtubule landscape to restrict AAV2 trafficking and identify microtubule detyrosination as a novel druggable target to improve AAV-based gene therapy. - Source: PubMed
Publication date: 2025/12/05
Tripathi ShefaliHuda ShamshulKar JoydiptaChandra DineshJayandharan Giridhara RMohan Nitin - Bladder cancer (BC) is a highly prevalent form of cancer worldwide, and cisplatin (CDDP) resistance poses a major challenge to patients. Cytoplasmic linker-associated protein 2 (CLASP2) is a member of the microtubule plus-end tracking protein family and is involved in the regulation of microtubule dynamics. In this study, we evaluated the influence of CLASP2 on BC progression and cisplatin resistance. Levels of CLASP2, HNRNPA1, NONO, ZRANB2, FUS, KHSRP and QKI in BC tissues and cells were tested by RT-qPCR. Protein levels of CLASP2 and KHSRP were detected by Western blot. Cell viability and IC50 of cisplatin-treated BC cells were measured by CCK-8. Cell proliferation and apoptosis were determined using colony formation assay and flow cytometry, respectively. RNA immunoprecipitation (RIP) and Co-immunoprecipitation (Co-IP) experiments were adopted to verify target genes of CLASP2. Cellular localization of CLASP2 and MAPRE1 was detected utilizing immunofluorescence staining. The xenograft tumor model was established in BALB/c nude mice. We found that iCLASP2 levels were increased in CDDP-resistant BC tissues and cells. Suppression of CLASP2 impeded BC cell proliferation and alleviated their resistance to CDDP. KHSRP positively influenced the stability of CLASP2 mRNA. There was a protein interaction between CLASP2 and MAPRE1. Silencing KHSRP or MAPRE1 reversed the effect exerted of CLASP2 on BC cells. CLASP2 decreased the sensitivity of BC to CDDP in vivo. Our results imply that CLASP2 contributes to tumorigenesis and cisplatin resistance in BC via targeting MAPRE1, thereby promoting BC progression and providing a new therapeutic target for BC treatment. - Source: PubMed
Publication date: 2025/05/17
Wang RuizheZhao ChengOu ZhenyuChen Lingxiao