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Acids Res. 2010 Aug; 38(14): 4821–4833. Published online 2010 Apr 5. doi:  10.1093/nar/gkq219PMCID: PMC2919719DNA-binding properties android external images media of T4 UvsY recombination mediator protein: polynucleotide wrapping promotes high-affinity binding to single-stranded DNAHang Xu, Hans T. H. Beernink, and Scott W. Morrical*Department of Biochemistry, content media external file 75555 Department of Microbiology and Molecular Genetics, and Vermont Cancer Center, University of Vermont College of Medicine, Burlington, VT 05405, USA*To whom correspondence should be addressed. Tel: Phone: +1 802 656 8260; Fax: +1 802 656 8220; Email: ude.mvu@acirromsPresent addresses: Hang Xu, Institute of Biophysics, Chinese Academy of Science, 15 Datun

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Road, Beijing 100101, People's Republic of China.Hans T.H. Beernink, BioSource International, 542 Flynn Road, Camarillo, CA 93012, USA.Author information ► Article notes ► Copyright and License information ►Received 2010 Feb 12; Revised 2010 Mar 15; Accepted 2010 Mar 16.Copyright © The Author(s) 2010. Published by Oxford University Press.This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.This article has been cited by other articles in PMC.AbstractTo carry out homologous recombination events in the cell, recombination proteins must be able to recognize and form presynaptic filaments on single-stranded DNA (ssDNA) in the presence of a vast excess of double-stranded DNA (dsDNA). Therefore recombination machineries stringently discriminate between ssDNA and dsDNA lattices. Recent single-molecule studies of bacteriophage T4 recombination proteins revealed that, s

us using cookies as described in About Cookies. You have free access to this contentJournal of NeurochemistryVolume 103, Issue 3, Version of Record online: 17 JUL 2007AbstractArticleReferences

Are a New Class of Microtubule-associated Protein (MAP) That Selectively Interacts with Assembled Microtubules via a Taxol-sensitive Binding Interaction* Pao-Chun Lin¶, Perry M. Chan‡, Christine Hall§ and Ed Manser‡¶,1 From the ‡Small G-protein Signaling http://www.jbc.org/content/286/48/41466.full and Kinases (sGSK-NRP) Group, Neuroscience Research Partnership, 61 Biopolis Drive, Singapore 138673, the https://www.researchgate.net/publication/26794444_CaMKII_phosphorylates_collapsin_response_mediator_protein_2_and_modulates_axonal_damage_during_glutamate_excitotoxicity ¶Institute of Medical Biology, 8A Biomedical Grove, Singapore 138648, and the §Institute of Neurology, University College London, 1 Wakefield Street, London WC1N 1PJ, United Kingdom ↵1 To whom correspondence should be addressed: Room 4-16B, Proteos, 61 Biopolis Dr., Singapore 138673. Tel.: 65-6586-9545; Fax: 65-67740742; E-mail: ed.manser{at}imb.a-star.edu.sg. Background: CRMPs play roles in axon content media specification and semaphorin 3A-induced growth cone collapse, but their biochemical function is unclear. Results: CRMPs are found to bind directly to microtubules through a conserved C-terminal region. Conclusion: CRMPs can stabilize microtubules but are negatively regulated by phosphorylation. Significance: This work can explain phenotypes associated with loss of CRMPs on axon specification and dendritic arborization.  Next Section Abstract Collapsin response mediator proteins are ubiquitously expressed content media external 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 neurodege

Google+ LinkedIn Reddit Download Full-text PDF CaMKII phosphorylates collapsin response mediator protein 2 and modulates axonal damage during glutamate excitotoxicityArticle (PDF Available) in Journal of Neurochemistry 111(3):870-81 · October 2009 with 26 ReadsDOI: 10.1111/j.1471-4159.2009.06375.x · Source: PubMed1st Shengtao Hou35.06 · South University of Science and Technology of China2nd Susan X Jiang31.25 · National Research Council Canada+ 53rd Amy AylsworthLast Kozo Kaibuchi50.5 · Nagoya UniversityShow more authorsAbstractIntracellular calcium influx through NMDA receptors triggers a cascade of deleterious signaling events which lead to neuronal death in neurological conditions such as stroke. However, it is not clear as to the molecular mechanism underlying early damage response from axons and dendrites which are important in maintaining a network essential for the survival of neurons. Here, we examined changes of axons treated with glutamate and showed the appearance of betaIII-tubulin positive varicosities on axons before the appearance of neuronal death. Dizocilpine blocked the occurrence of varicosities on axons suggesting that these microstructures were mediated by NMDA receptor activities. Despite early increased expression of pCaMKII and pMAPK after just 10 min of glutamate treatment, only inhibitors to Ca(2+)/calmodulin-dependent protein kinase II (CaMKII) and calpain prevented the occurrence of axonal varicosities. In contrast, inhibitors to Rho kinase, mitogen-activated protein kinase and phosphoinositide 3-kinase were not effective, nor were they able to rescue neurons from death, suggesting CaMKII and calpain are important in axon survival. Activated CaMKII directly phosphorylates collapsin response mediator protein (CRMP) 2 which is independent of calpain-mediated cleavage of CRMP2. Over-expression of CRMP2, but not the phosphorylation-resistant mutant CRMP2-T555A, increased axonal resistance to glutamate toxicity with reduced numbers of va