GSK-3 mediates the okadaic acid-induced modification of collapsin response mediator protein-2 in human SK-N-SH neuroblastoma cells

2008 ◽  
Vol 103 (6) ◽  
pp. 1833-1848 ◽  
Author(s):  
Mei-Hui Ni ◽  
Chih-Ching Wu ◽  
Wen-Hsiung Chan ◽  
Kun-Yi Chien ◽  
Jau-Song Yu
Keyword(s):  
Okadaic Acid ◽  
Neuroblastoma Cells ◽  
Collapsin Response Mediator Protein ◽  
Mediator Protein

scholarly journals Collapsin Response Mediator Protein Switches RhoA and Rac1 Morphology in N1E-115 Neuroblastoma Cells and Is Regulated by Rho Kinase

2001 ◽  
Vol 276 (46) ◽  
pp. 43482-43486 ◽  
Author(s):  
Christine Hall ◽  
Matthew Brown ◽  
Tom Jacobs ◽  
Giovanna Ferrari ◽  
Nansi Cann ◽  
...  
Keyword(s):  
Neuroblastoma Cells ◽  
Rho Kinase ◽  
Collapsin Response Mediator Protein ◽  
Mediator Protein

scholarly journals CRMP2 Is Involved in Regulation of Mitochondrial Morphology and Motility in Neurons

Cells ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 2781
Author(s):  
Tatiana Brustovetsky ◽  
Rajesh Khanna ◽  
Nickolay Brustovetsky
Keyword(s):  
Okadaic Acid ◽  
Light Chain ◽  
Small Interfering Rna ◽  
Mitochondrial Fission ◽  
Mitochondrial Morphology ◽  
Related Protein ◽  
Phosphorylation State ◽  
Collapsin Response Mediator Protein ◽  
Mediator Protein ◽  
Interfering Rna

Regulation of mitochondrial morphology and motility is critical for neurons, but the exact mechanisms are unclear. Here, we demonstrate that these mechanisms may involve collapsin response mediator protein 2 (CRMP2). CRMP2 is attached to neuronal mitochondria and binds to dynamin-related protein 1 (Drp1), Miro 2, and Kinesin 1 light chain (KLC1). Treating neurons with okadaic acid (OA), an inhibitor of phosphatases PP1 and PP2A, resulted in increased CRMP2 phosphorylation at Thr509/514, Ser522, and Thr555, and augmented Drp1 phosphorylation at Ser616. The CRMP2-binding small molecule (S)-lacosamide ((S)-LCM) prevented an OA-induced increase in CRMP2 phosphorylation at Thr509/514 and Ser522 but not at Thr555, and also failed to alleviate Drp1 phosphorylation. The increased CRMP2 phosphorylation correlated with decreased CRMP2 binding to Drp1, Miro 2, and KLC1. (S)-LCM rescued CRMP2 binding to Drp1 and Miro 2 but not to KLC1. In parallel with CRMP2 hyperphosphorylation, OA increased mitochondrial fission and suppressed mitochondrial traffic. (S)-LCM prevented OA-induced alterations in mitochondrial morphology and motility. Deletion of CRMP2 with a small interfering RNA (siRNA) resulted in increased mitochondrial fission and diminished mitochondrial traffic. Overall, our data suggest that the CRMP2 expression level and phosphorylation state are involved in regulating mitochondrial morphology and motility in neurons.

scholarly journals Spastin interacts with CRMP5 to promote spindle organization in mouse oocytes by severing microtubules

Zygote ◽  
2021 ◽  
pp. 1-12
Author(s):  
Zhen Jin ◽  
Hua-Feng Shou ◽  
Jin-Wei Liu ◽  
Shan-Shan Jiang ◽  
Yan Shen ◽  
...  
Keyword(s):  
Developmental Disorders ◽  
Spindle Microtubule ◽  
Collapsin Response Mediator Protein ◽  
Microtubule Severing ◽  
Structural Support ◽  
Mediator Protein ◽  
Spindle Microtubules ◽  
Transportation Routes ◽  
Normal Meiosis

Abstract Microtubule-severing protein (MTSP) is critical for the survival of both mitotic and postmitotic cells. However, the study of MTSP during meiosis of mammalian oocytes has not been reported. We found that spastin, a member of the MTSP family, was highly expressed in oocytes and aggregated in spindle microtubules. After knocking down spastin by specific siRNA, the spindle microtubule density of meiotic oocytes decreased significantly. When the oocytes were cultured in vitro, the oocytes lacking spastin showed an obvious maturation disorder. Considering the microtubule-severing activity of spastin, we speculate that spastin on spindles may increase the number of microtubule broken ends by severing the microtubules, therefore playing a nucleating role, promoting spindle assembly and ensuring normal meiosis. In addition, we found the colocalization and interaction of collapsin response mediator protein 5 (CRMP5) and spastin in oocytes. CRMP5 can provide structural support and promote microtubule aggregation, creating transportation routes, and can interact with spastin in the microtubule activity of nerve cells (30). Knocking down CRMP5 may lead to spindle abnormalities and developmental disorders in oocytes. Overexpression of spastin may reverse the abnormal phenotype caused by the deletion of CRMP5. In summary, our data support a model in which the interaction between spastin and CRMP5 promotes the assembly of spindle microtubules in oocytes by controlling microtubule dynamics, therefore ensuring normal meiosis.

The protein interactome of collapsin response mediator protein-2 (CRMP2/DPYSL2) reveals novel partner proteins in brain tissue

2015 ◽  
Vol 9 (9-10) ◽  
pp. 817-831 ◽  
Author(s):  
Daniel Martins-de-Souza ◽  
Juliana S. Cassoli ◽  
Juliana M. Nascimento ◽  
Kenneth Hensley ◽  
Paul C. Guest ◽  
...  
Keyword(s):  
Brain Tissue ◽  
Collapsin Response Mediator Protein ◽  
Protein Interactome ◽  
Mediator Protein ◽  
Partner Proteins

scholarly journals Genetic suppression of collapsin response mediator protein 2 phosphorylation improves outcome in methyl-4-phenyl-1,2,3,6-tetrahydropyridine-induced Parkinson’s model mice

2018 ◽  
Vol 24 (1) ◽  
pp. 31-40 ◽  
Author(s):  
Kentaro Togashi ◽  
Masaya Hasegawa ◽  
Jun Nagai ◽  
Aine Tonouchi ◽  
Daiki Masukawa ◽  
...  
Keyword(s):  
Collapsin Response Mediator Protein ◽  
Mediator Protein ◽  
Genetic Suppression

scholarly journals Loss of CRMP2 O-GlcNAcylation leads to reduced novel object recognition performance in mice

Open Biology ◽  
2019 ◽  
Vol 9 (11) ◽  
pp. 190192 ◽  
Author(s):  
Villo Muha ◽  
Ritchie Williamson ◽  
Rachel Hills ◽  
Alison D. McNeilly ◽  
Thomas G. McWilliams ◽  
...  
Keyword(s):  
Nervous System ◽  
Memory Impairment ◽  
Recognition Performance ◽  
Novel Object Recognition ◽  
Small Decrease ◽  
Post Translational Modification ◽  
Site Specific ◽  
Novel Object ◽  
Collapsin Response Mediator Protein ◽  
Mediator Protein

O-GlcNAcylation is an abundant post-translational modification in the nervous system, linked to both neurodevelopmental and neurodegenerative disease. However, the mechanistic links between these phenotypes and site-specific O-GlcNAcylation remain largely unexplored. Here, we show that Ser517 O-GlcNAcylation of the microtubule-binding protein Collapsin Response Mediator Protein-2 (CRMP2) increases with age. By generating and characterizing a Crmp2 S517A knock-in mouse model, we demonstrate that loss of O-GlcNAcylation leads to a small decrease in body weight and mild memory impairment, suggesting that Ser517 O-GlcNAcylation has a small but detectable impact on mouse physiology and cognitive function.

Sign in / Sign up

Export Citation Format

Share Document