Mammalian microtubule P-body dynamics are mediated by nesprin-1
Open accessAbstract
Nesprins are a multi-isomeric family of spectrin-repeat (SR) proteins, predominantly known as nuclear envelope scaffolds. However, isoforms that function beyond the nuclear envelope remain poorly examined. Here, we characterize p50(Nesp1), a 50-kD isoform that localizes to processing bodies (PBs), where it acts as a microtubule-associated protein capable of linking mRNP complexes to microtubules. Overexpression of dominant-negative p50(Nesp1) caused Rck/p54, but not GW182, displacement from microtubules, resulting in reduced PB movement and cross talk with stress granules (SGs). These cells disassembled canonical SGs induced by sodium arsenite, but not those induced by hydrogen peroxide, leading to cell death and revealing PB-microtubule attachment is required for hydrogen peroxide-induced SG anti-apoptotic functions. Furthermore, p50(Nesp1) was required for miRNA-mediated silencing and interacted with core miRISC silencers Ago2 and Rck/p54 in an RNA-dependent manner and with GW182 in a microtubule-dependent manner. These data identify p50(Nesp1) as a multi-functional PB component and microtubule scaffold necessary for RNA granule dynamics and provides evidence for PB and SG micro-heterogeneity.
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Disruption of nesprin-1 activity through mutations and RNAi significantly decreased miRNA suppression of target mRNA and P-body formation.
“Disruption of nesprin-1 activity through mutations and RNAi significantly decreased miRNA suppression of target mRNA and P-body formation.”
From Overview of MicroRNA Biogenesis, Mechanisms of Actions, and Circulation (2018) · cites this paper as [81]
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Stress granules and processing bodies are dynamically linked sites of mRNP remodeling
Kedersha, N., Stoecklin, G., Ayodele, M. O., Yacono, P. W., Lykke‐Andersen, J., Fritzler, M. J., Scheuner, D. L., Kaufman, R. J., Golan, D. E., & Anderson, P. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200502088 · Cited by 1,494 · see citing works
Self-citationDecapping and Decay of Messenger RNA Occur in Cytoplasmic Processing Bodies
Sheth, U., & Parker, R. (2003) · Science · doi:10.1126/science.1082320 · Cited by 1,372 · see citing works
Coupling of the nucleus and cytoplasm: Role of the LINC complex
Crisp, M., Liu, Q., Roux, K. J., Rattner, J. B., Shanahan, C. M., Burke, B. E., Stahl, P. D., & Hodzic, D. M. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200509124 · Cited by 1,339 · see citing works
Self-citationTarget mRNAs are repressed as efficiently by microRNA-binding sites in the 5′ UTR as in the 3′ UTR
Lytle, J., Yario, T. A., & STEITZ, J. A. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703820104 · Cited by 1,196 · see citing works
Stress granules: the Tao of RNA triage.
Anderson, P., & Kedersha, N. (2008) · TIBS -Trends in Biochemical Sciences. Regular ed · doi:10.1016/j.tibs.2007.12.003 · Cited by 1,156 · see citing works
P bodies: at the crossroads of post-transcriptional pathways
Eulálio, A., Behm‐Ansmant, I., & Izaurralde, E. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2080 · Cited by 939 · see citing works
Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
Bernardi, R., & Pandolfi, P. P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2277 · Cited by 876 · see citing works
Movement of Eukaryotic mRNAs Between Polysomes and Cytoplasmic Processing Bodies
Brengues, M., Teixeira, D., & Parker, R. (2005) · Science · doi:10.1126/science.1115791 · Cited by 796 · see citing works
P-body formation is a consequence, not the cause, of RNA-mediated gene silencing
Eulalio, A., Behm-Ansmant, I., Schweizer, D., & Izaurralde, E. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00128-07 · Cited by 710 · see citing works
Formation of stress granules inhibits apoptosis by suppressing stress-responsive MAPK pathways
有本, 京., Fukuda, H., Imajoh‐Ohmi, S., Saito, H., & Takekawa, M. (2008) · Nature Cell Biology · doi:10.1038/ncb1791 · Cited by 607 · see citing works
Translation Repression in Human Cells by MicroRNA-Induced Gene Silencing Requires RCK/p54
Chu, C., & Rana, T. M. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040210 · Cited by 521 · see citing works
Wilhelmsen, K., Litjens, S. H. M., Kuikman, I., Tshimbalanga, N., Janssen, H., van den Bout, I., Raymond, K., & Sonnenberg, A. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200506083 · Cited by 483 · see citing works
Zhang, Q., Skepper, J. N., Yang, F., Davies, J. D., Hegyi, L., Roberts, R. G., Weissberg, P. L., Ellis, J. A., & Shanahan, C. M. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.24.4485 · Cited by 418 · see citing works
Self-citationPolysomes, P bodies and stress granules: states and fates of eukaryotic mRNAs
Balagopal, V., & Parker, R. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.03.005 · Cited by 391 · see citing works
Cellular MicroRNA and P Bodies Modulate Host-HIV-1 Interactions
Nathans, R. S., Chu, C., Serquiña, A., Lu, C., Cao, H., & Rana, T. M. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.06.003 · Cited by 373 · see citing works
Eystathioy, T., Chan, E. K. L., Tenenbaum, S. A., Keene, J. D., Griffith, K. J., & Fritzler, M. J. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-11-0544 · Cited by 363 · see citing works
Self-citationNesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization
Roux, K. J., Crisp, M., Liu, Q., Kim, D., Козлов, С. В., Stewart, C. L., & Burke, B. E. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808602106 · Cited by 358 · see citing works
Mutations in SYNE1 lead to a newly discovered form of autosomal recessive cerebellar ataxia
Gros‐Louis, F., Dupré, N., Dion, P. A., Fox, M. A., Laurent, S. B., Verreault, S., Sanes, J. R., Bouchard, J.-P., & Rouleau, G. A. (2006) · Nature Genetics · doi:10.1038/ng1927 · Cited by 347 · see citing works
Nonhoff, U., Ralser, M., Welzel, F., Piccini, I., Balzereit, D., Yaspo, M., Lehrach, H. R., & Krobitsch, S. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-12-1120 · Cited by 347 · see citing works
Direct interaction of microtubule- and actin-based transport motors
Huang, J., Brady, S. T., Richards, B. W., Stenoien, D. L., Resau, J. H., Copeland, N. G., & Jenkins, N. A. (1999) · Nature · doi:10.1038/16722 · Cited by 334 · see citing works
Anderson, P., & Kedersha, N. (2009) · Current Biology · doi:10.1016/j.cub.2009.03.013 · Cited by 302 · see citing works
Subramanian, R., Kubalek, E. W., Arthur, C. P., Bick, M. J., Campbell, E. A., Darst, S. A., Milligan, R. A., & Kapoor, T. M. (2010) · Cell · doi:10.1016/j.cell.2010.07.012 · Cited by 301 · see citing works
Stewart-Hutchinson, P. J., Hale, C. M., Wirtz, D., & Hodzic, D. M. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.02.022 · Cited by 287 · see citing works
The spectrin repeat: a structural platform for cytoskeletal protein assemblies
Djinović‐Carugo, K., Gautel, M., Ylänne, J., & Young, P. W. (2002) · FEBS Letters · doi:10.1016/s0014-5793(01)03304-x · Cited by 286 · see citing works
Zhang, Q., Ragnauth, C. D., Skepper, J. N., Worth, N. F., Warren, D. T., Roberts, R. G., Weissberg, P. L., Ellis, J. A., & Shanahan, C. M. (2005) · Journal of Cell Science · doi:10.1242/jcs.01642 · Cited by 277 · see citing works
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The Dynamics of Mammalian P Body Transport, Assembly, and Disassembly In Vivo
Aizer, A., Brody, Y., Ler, L. W., Sonenberg, N., Singer, R. H., & Shav‐Tal, Y. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-05-0513 · Cited by 227 · see citing works
Zhang, Q., Ragnauth, C. D., Greener, M., Shanahan, C. M., & Roberts, R. G. (2002) · Genomics · doi:10.1006/geno.2002.6859 · Cited by 209 · see citing works
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Horn, H. F., Brownstein, Z., Lenz, D. R., Shivatzki, S., Dror, A. A., Dagan‐Rosenfeld, O., Friedman, L. M., Roux, K. J., Kozlov, S. V., Jeang, K., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci66911 · Cited by 168 · see citing works
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Mellad, J. A., Warren, D. T., & Shanahan, C. M. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.11.006 · Cited by 162 · see citing works
Self-citationSavas, J. N., Makusky, A. J., Ottosen, S., Baillat, D., Then, F., Krainc, D., Shiekhattar, R., Markey, S. P., & Tanese, N. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800658105 · Cited by 160 · see citing works
Ketema, M., Wilhelmsen, K., Kuikman, I., Janssen, H., Hodzic, D. M., & Sonnenberg, A. (2007) · Journal of Cell Science · doi:10.1242/jcs.014191 · Cited by 155 · see citing works
Hydrogen peroxide induces stress granule formation independent of eIF2α phosphorylation
Emara, M. M., Fujimura, K., Sciaranghella, D., Ivanova, V., Ivanov, P. V., & Anderson, P. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.06.033 · Cited by 153 · see citing works
Laughlin, R. C., & Temesvari, L. A. (2005) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399405009622 · Cited by 149 · see citing works
Minshall, N., Kress, M., Barbieri-Weill, D., & Standart, N. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-01-0035 · Cited by 130 · see citing works
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Warren, D. T., Zhang, Q., Weissberg, P. L., & Shanahan, C. M. (2005) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399405009294 · Cited by 116 · see citing works
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Self-citationCottrell, J. R., Borók, E., Horváth, T. L., & Nedivi, E. (2004) · Neuron · doi:10.1016/j.neuron.2004.10.025 · Cited by 108 · see citing works
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Moser, J. J., & Fritzler, M. J. (2009) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2009.11.018 · Cited by 97 · see citing works
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Warren, D. T., Tajsic, T., Mellad, J. A., Searles, R. G., Zhang, Q., & Shanahan, C. M. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.032557 · Cited by 58 · see citing works
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Affaitati, A., de Cristofaro, T., Feliciello, A., & Varrone, S. (2001) · Gene · doi:10.1016/s0378-1119(01)00402-4 · Cited by 29 · see citing works
Kobayashi, Y., Katanosaka, Y., Iwata, Y. T., Matsuoka, M., Shigekawa, M., & Wakabayashi, S. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.06.026 · Cited by 28 · see citing works
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Lindsay, A. J., & McCaffrey, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.182808 · Cited by 20 · see citing works
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Castilla‐Llorente, V., Spraggon, L., Okamura, M., Naseeruddin, S., Adamow, M. J., Qamar, S., & Liu, J. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201201153 · Cited by 15 · see citing works
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Self-citation
- Authors
- Rajgor, D., Mellad, J. A., Soong, D., Rattner, J. B., Fritzler, M. J., & Shanahan, C. M.
- Affiliations
- King's College London (GB)
- University of Calgary (CA)
- Corresponding author
- Shanahan, Catherine M.
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2014-05-26
- Volume
- 205
- Issue
- 4
- Pages
- 457-475
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC4033771
- OpenAlex
- W2043148470
- Cited by
- 26
- References
- 52
- Citations by year
- 2025: 1 · 2024: 3 · 2022: 1 · 2020: 1 · 2018: 3 · 2017: 2 · 2016: 5 · 2015: 8 · 2014: 2
- FWCI
- 2.32
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Edinburgh Research Explorer (University of Edinburgh) (publishedVersion, other-oa)
- Research Portal (King's College London) (submittedVersion)
- Funders
- British Heart Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- nesprin-1, P-bodies, microtubules, stress granules, GW182, miRNA-induced silencing complex, Argonaute 2, messenger ribonucleoprotein, sodium arsenite, hydrogen peroxide, apoptosis
- MeSH terms
- Animals, Cytoplasmic Granules, Cytoskeletal Proteins, Enzyme Inhibitors, Fibroblasts, Humans, Hydrogen Peroxide, Mammals, Microtubules, Muscle, Smooth, Vascular, Nerve Tissue Proteins, Nuclear Proteins, RNA, Messenger, Osteosarcoma, Stress, Physiological, Oxidants, Sodium Compounds, Arsenites, Dermis, Myoblasts, Cell Line, Tumor, Mice, Gene Knockdown Techniques
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