Author Correction: Activation of the unfolded protein response promotes axonal regeneration after peripheral nerve injury (Scientific Reports, (2016), 6, 1, (21709), 10.1038/srep21709);Activation of the unfolded protein response promotes axonal regeneration after peripheral nerve injury

Scientific Reports

Volumn 6, Issue , 2016, Pages

  Oñate, Maritza ^a,b,c,d   Catenaccio, Alejandra ^a,b   Martínez, Gabriela ^a,b,c,d   Armentano, Donna ^e   Parsons, Geoffrey ^e   Kerr, Bredford ^f   Hetz, Claudio ^a,c,d,g   Court, Felipe A ^a,b  

^a Universidad de Chile and Geroscience Center for Brain Health and Metabolism   (Chile)

^b PONTIFICIA UNIVERSIDAD CATÓLICA DE CHILE   (Chile)

^c UNIVERSITY OF CHILE   (Chile)

^d UNIVERSITY OF CHILE   (Chile)

^e GENZYME CORPORATION   (United States)

^f CENTRO DE ESTUDIOS CIENTÍFICOS CECS   (Chile)

^g HARVARD SCHOOL OF PUBLIC HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ATF4 PROTEIN, HUMAN; CCL2 PROTEIN, MOUSE; MONOCYTE CHEMOTACTIC PROTEIN 1; X BOX BINDING PROTEIN 1; XBP1 PROTEIN, MOUSE;

ANIMAL; AXON; C57BL MOUSE; CONVALESCENCE; ENDOPLASMIC RETICULUM STRESS; GENE EXPRESSION; GENETICS; INJURIES; KNOCKOUT MOUSE; LOCOMOTION; MACROPHAGE; METABOLISM; NERVE REGENERATION; PATHOPHYSIOLOGY; PERIPHERAL NERVE INJURY; PHYSIOLOGY; SCIATIC NERVE; UNFOLDED PROTEIN RESPONSE;

ACTIVATING TRANSCRIPTION FACTOR 4; ANIMALS; AXONS; CHEMOKINE CCL2; ENDOPLASMIC RETICULUM STRESS; GENE EXPRESSION; LOCOMOTION; MACROPHAGES; MICE, INBRED C57BL; MICE, KNOCKOUT; NERVE REGENERATION; PERIPHERAL NERVE INJURIES; RECOVERY OF FUNCTION; SCIATIC NERVE; UNFOLDED PROTEIN RESPONSE; X-BOX BINDING PROTEIN 1;

EID: 84959432869     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/s41598-021-04003-2     Document Type: Erratum

References (62)

1. Chen, Z.-L., Yu, W.-M. & Strickland, S. Peripheral regeneration. Annu. Rev. Neurosci. 30, 209-33 (2007).
2. Lutz, A. B. & Barres, B. A. Contrasting the glial response to axon injury in the central and peripheral nervous systems. Dev. Cell 28, 7-17 (2014).
3. Waller, A. Experiments on the section of the glossopharyngeal and hypoglossal nerves of the frog, and observations of the alterations prduced thereby in the structure of their primitive fibres. Philos. Trans. R. Soc. B Biol. Sci. 140, 423-429 (1850).
4. Court, F. A. & Coleman, M. P. Mitochondria as a central sensor for axonal degenerative stimuli. Trends Neurosci. 35, 364-72 (2012).
5. Arthur-Farraj, P. J. et al. c-Jun reprograms Schwann cells of injured nerves to generate a repair cell essential for regeneration. Neuron 75, 633-47 (2012).
6. Glenn, T. D. & Talbot, W. S. Signals regulating myelination in peripheral nerves and the Schwann cell response to injury. Curr. Opin. Neurobiol. 23, 1041-8 (2013).
7. Sofroniew, M. V. Molecular dissection of reactive astrogliosis and glial scar formation. Trends Neurosci. 32, 638-647 (2009).
8. Li, S., Yang, L. & Selzer, M. E. Neuronal endoplasmic reticulum stress in axon injury and neurodegeneration. Ann. Neurol. 74, 768-777 (2013).
9. Hetz, C., Chevet, E. & Oakes, S. A. Proteostasis control by the unfolded protein response. Nat. Cell Biol. 17, 829-38 (2015).
10. Acosta-Alvear, D. et al. XBP1 Controls Diverse Transcriptional Regulatory Networks. Mol. Cell 27, 53-66 (2007).
11. Harding, H. P. et al. An integrated stress response regulates amino acid metabolism and resistance to oxidative stress. Mol. Cell 11, 619-633 (2003).
12. Urra, H., Dufey, E., Lisbona, F., Rojas-Rivera, D. & Hetz, C. When ER stress reaches a dead end. Biochim. Biophys. Acta 1833, 3507-17 (2013).
13. Hetz, C. & Mollereau, B. Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases. Nat. Rev. Neurosci. 15, 233-49 (2014).
14. Valenzuela, V. et al. Activation of the unfolded protein response enhances motor recovery after spinal cord injury. Cell Death Dis. 3, e272 (2012).
15. Ohri, S. S., Hetman, M. & Whittemore, S. R. Restoring endoplasmic reticulum homeostasis improves functional recovery after spinal cord injury. Neurobiol. Dis. 58, 29-37 (2013).
16. Ohri, S. S., Mullins, A., Hetman, M. & Whittemore, S. R. Inhibition of GADD34, the stress-inducible regulatory subunit of the endoplasmic reticulum stress response, does not enhance functional recovery after spinal cord Injury. PLoS One 9, e109703 (2014).
17. Castillo, V. et al. Functional Role of the Disulfide Isomerase ERp57 in Axonal Regeneration. PLoS One 10, e0136620 (2015).
18. Saxena, S., Cabuy, E. & Caroni, P. A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice. Nat. Neurosci. 12, 627-36 (2009).
19. Penas, C. et al. Autophagy, and BiP level decrease are early key events in retrograde degeneration of motoneurons. Cell Death Differ. 18, 1617-27 (2011).
20. Ying, Z. et al. The Unfolded Protein Response and Cholesterol Biosynthesis Link Luman/CREB3 to Regenerative Axon Growth in Sensory Neurons. J. Neurosci. 35, 14557-14570 (2015).
21. Fawcett, J. W. & Keynes, R. J. Peripheral nerve regeneration. Annu. Rev. Neurosci. 13, 43-60 (1990).
22. Kakiuchi, C., Ishiwata, M., Hayashi, A. & Kato, T. XBP1 induces WFS1 through an endoplasmic reticulum stress response elementlike motif in SH-SY5Y cells. J. Neurochem. 97, 545-555 (2006).
23. Hetz, C. et al. Unfolded protein response transcription factor XBP-1 does not influence prion replication or pathogenesis. PNAS 105, 757-762 (2008).
24. Masuoka, H. C. & Townes, T. M. Targeted disruption of the activating transcription factor 4 gene results in severe fetal anemia in mice. Blood 99, 736-745 (2002).
25. Martínez, G. et al. Regulation of memory formation by the transcription factor XBP1. Cell reports. doi:10.1016/j.celrep.2016.01.028 (2016).
26. Perrin, F. E., Lacroix, S., Avilés-Trigueros, M. & David, S. Involvement of monocyte chemoattractant protein-1, macrophage inflammatory protein-1alpha and interleukin-1beta in Wallerian degeneration. Brain 128, 854-66 (2005).
27. Valdés, P. et al. Control of dopaminergic neuron survival by the unfolded protein response transcription factor XBP1. PNAS 111, 6804-9 (2014).
28. Rigaud, M. et al. Species and strain differences in rodent sciatic nerve anatomy; Implications for studies of neuropathic pain. Pain 136, 188-201 (2008).
29. Villegas, R. et al. Calcium release from intra-axonal endoplasmic reticulum leads to axon degeneration through mitochondrial dysfunction. J. Neurosci. 34, 7179-89 (2014).
30. Barrientos, S. et al. Axonal degeneration is mediated by the mitochondrial permeability transition pore. J. Neurosci. 31, 966-978 (2011).
31. Calixto, A., Jara, J. S. & Court, F. A. Diapause formation and downregulation of insulin-like signaling via DAF-16/FOXO delays axonal degeneration and neuronal loss. PLoS Genet. 8, e1003141 (2012).
32. Mantuano, E. et al. The unfolded protein response is a major mechanism by which LRP1 regulates Schwann cell survival after injury. J. Neurosci. 31, 13376-85 (2011).
33. Phay, M., Kim, H. H. & Yoo, S. Dynamic Change and Target Prediction of Axon-Specific MicroRNAs in Regenerating Sciatic Nerve. PLoS One 10, e0137461 (2015).
34. Pennuto, M. et al. Ablation of the UPR-mediator CHOP restores motor function and reduces demyelination in Charcot-Marie-Tooth 1B mice. Neuron 57, 393-405 (2008).
35. D'Antonio, M. et al. Resetting translational homeostasis restores myelination in Charcot-Marie-Tooth disease type 1B mice. J. Exp. Med. 210, 821-38 (2013).
36. Jung, H., Yoon, B. & Holt, C. Axonal mRNA localization and local protein synthesis in nervous system assembly, maintenance and repair. Nat. Rev. Neurosci. 13, 308-324 (2012).
37. Ying, Z., Misra, V. & Verge, V. Sensing nerve injury at the axonal ER: Activated Luman/CREB3 serves as a novel axonally synthesized retrograde regeneration signal. PNAS 111, 16142-7 (2014).
38. Shoulders, M. et al. Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environments. Cell Rep. 3, 1279-92 (2013).
39. Yoshida, H., Matsui, T., Yamamoto, A., Okada, T. & Mori, K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 107, 881-891 (2001).
40. Hu, Y. et al. Differential effects of unfolded protein response pathways on axon injury-induced death of retinal ganglion cells. Neuron 73, 445-52 (2012).
41. Hetz, C. et al. XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy. Genes Dev. 23, 2294-2306 (2009).
42. Matus, S., Lopez, E., Valenzuela, V., Nassif, M. & Hetz, C. Functional contribution of the transcription factor ATF4 to the pathogenesis of amyotrophic lateral sclerosis. PLoS One 8, e66672 (2013).
43. Vidal, R. et al. Targeting the UPR transcription factor XBP1 protects against Huntington's disease through the regulation of FoxO1 and autophagy. Hum. Mol. Genet. 21, 2245-2262 (2012).
44. Moreno, J. A. et al. Oral treatment targeting the Unfolded Protein Response prevents neurodegeneration and clinical disease in prion-infected mice. Sci. Transl. Med. 5, 206ra138 (2013).
45. Park, H. & Poo, M. Neurotrophin regulation of neural circuit development and function. Nat. Rev. Neurosci. 14, 7-23 (2012).
46. Cornejo, V. H., Pihán, P., Vidal, R. L. & Hetz, C. Role of the unfolded protein response in organ physiology: lessons from mouse models. IUBMB Life 65, 962-75 (2013).
47. Reimold, A. M. et al. Plasma cell differentiation requires the transcription factor XBP-1. Nature 412, 300-307 (2001).
48. Iwakoshi, N. N. et al. Plasma cell differentiation and the unfolded protein response intersect at the transcription factor XBP-1. Nat. Immunol. 4, 321-9 (2003).
49. Huh, W. J. et al. XBP1 controls maturation of gastric zymogenic cells by induction of MIST1 and expansion of the rough endoplasmic reticulum. Gastroenterology 139, 2038-2049 (2010).
50. Lee, A.-H., Chu, G. C., Iwakoshi, N. N. & Glimcher, L. H. XBP-1 is required for biogenesis of cellular secretory machinery of exocrine glands. EMBO J. 24, 4368-80 (2005).
51. Hetz, C., Martinon, F., Rodriguez, D. & Glimcher, L. The unfolded protein response: integrating stress signals through the stress sensor IRE1α. Physiol. Rev. 91, 1219-43 (2011).
52. Tsang, K. Y. et al. Surviving endoplasmic reticulum stress is coupled to altered chondrocyte differentiation and function. PLoS Biol. 5, e44 (2007).
53. Del Vecchio, C. A. et al. De-differentiation confers multidrug resistance via noncanonical PERK-Nrf2 signaling. PLoS Biol. 12, e1001945 (2014).
54. Wielenga, M. C. B. et al. ER-Stress-Induced Differentiation Sensitizes Colon Cancer Stem Cells to Chemotherapy. Cell Rep. 13, 489-494 (2015).
55. Patzig, J. et al. Quantitative and integrative proteome analysis of peripheral nerve myelin identifies novel myelin proteins and candidate neuropathy loci. J. Neurosci. 31, 16369-86 (2011).
56. Lin, W. & Popko, B. Endoplasmic reticulum stress in disorders of myelinating cells. Nat. Neurosci. 12, 379-385 (2009).
57. Martinon, F. & Glimcher, L. H. Regulation of innate immunity by signaling pathways emerging from the endoplasmic reticulum. Curr. Opin. Immunol. 23, 35-40 (2011).
58. Tofaris, G. K., Patterson, P. H., Jessen, K. R. & Mirsky, R. Denervated Schwann cells attract macrophages by secretion of Leukemia Inhibitory Factor (LIF) and Monocyte Chemoattractant Protein-1 in a process regulated by interleukin-6 and LIF. J. Neurosci. 22, 6696-6703 (2002).
59. Hetz, C., Chevet, E. & Harding, H. Targeting the unfolded protein response in disease. Nat. Rev. Drug Discov. 12, 703-19 (2013).
60. Borchelt, D. et al. A vector for expressing foreign genes in the brains and hearts of transgenic mice. Genet. Anal. Biomol. Eng. 13, 159-163 (1996).
61. Rodriguez, D. A. et al. BH3-only proteins are part of a regulatory network that control the sustained signalling of the unfolded protein response sensor IRE1α. EMBO J. 31, 2322-35 (2012).
62. Inserra, M., Bloch, D. & Terris, D. Functional indices for sciatic, peroneal, and posterior tibial nerve lesions in the mouse. Microsurgery 18, 119-24 (1998).