The reticulons: Guardians of the structure and function of the endoplasmic reticulum

Experimental Cell Research

Volumn 318, Issue 11, 2012, Pages 1201-1207

  Di Sano, Federica ^a   Bernardoni, Paolo ^a   Piacentini, Mauro ^a,b  

^a UNIVERSITY OF ROME TOR VERGATA   (Italy)

^b NATIONAL INSTITUTE FOR INFECTIOUS DISEASES L SPALLANZANI   (Italy)

Author keywords

Apoptosis; ER stress; Neurodegeneration; Reticulons

Indexed keywords

CALCIUM; MEMBRANE PROTEIN; PROTEIN; PROTEIN DP1; RETICULON; SECRETORY PROTEIN; UNCLASSIFIED DRUG;

CALCIUM CELL LEVEL; CELL DIFFERENTIATION; CELL DIVISION; DISULFIDE BOND; ENDOPLASMIC RETICULUM; HUMAN; MEMBRANE STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; REVIEW;

EID: 84861673568     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2012.03.002     Document Type: Review

References (51)

1. Teng F.Y., Tang B.L. Cell autonomous function of Nogo and reticulons: the emerging story at the endoplasmic reticulum. J. Cell. Physiol. 2008, 216:303-308.
2. Oertle T., Klinger M., Stuermer C.A., Schwab M.E. A reticular rhapsody: phylogenic evolution and nomenclature of the RTN/Nogo gene family. FASEB J. 2003, 17:1238-1247.
3. Yang Y.S., Strittmatter S.M. The reticulons: a family of proteins with diverse functions. Genome Biol. 2007, 8:234.
4. Oertle T., Van der Haar M.E., Bandtlow C.E., Robeva A., Burfeind P., Buss A., Huber A.B., Simonen M., Schnell L., Brsamle C., Kaupmann K., Vallon R., Schwab M.E. Nogo-A inhibits neurite outgrowth and cell spreading with three discrete regions. J. Neurosci. 2003, 23:5393-5406.
5. He W., Shi Q., Hu X., Yan R. The membrane topology of RTN3 and its effect on binding of RTN3 to BACE1. J. Biol. Chem. 2007, 282:29144-29151.
6. Brandizzi F., Frangne N., Marc-Martin S., Hawes C., Neuhaus J.M., Paris N. The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain. Plant Cell 2002, 14:1077-1092.
7. Bauer M., Pelkmans L. A new paradigm for membrane-organizing and -shaping scaffolds. FEBS Lett. 2006, 580:5559-5564.
8. Tolley N., Sparkes I., Craddock C.P., Eastmond P.J., Runions J., Hawes C., Frigerio L. Transmembrane domain length is responsible for the ability of a plant reticulon to shape endoplasmic reticulum tubules in vivo. Plant J. 2010, 64:411-418.
9. Sparkes I., Tolley N., Aller I., Svozil J., Osterrieder A., Botchway S., Mueller C., Frigerio L., Hawes C. Five Arabidopsis reticulon isoforms share endoplasmic reticulum location, topology, and membrane-shaping properties. Plant Cell 2010, 22:1333-1343.
10. Shibata Y., Voss C., Rist J.M., Hu J., Rapoport T.A., Prinz W.A., Voeltz G.K. The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum. J. Biol. Chem. 2008, 283:18892-18904.
11. Hu J., Shibata Y., Voss C., Shemesh T., Li Z., Couglin M., Kozlov M.M., Rapoport T.A., Prinz W.A. Membrane proteins of the endoplasmic reticulum induce high-curvature tubules. Science 2008, 319:1247-1250.
12. Voeltz G.K., Prinz W.A., Shibata Y., Rist J.M., Rapoport T.A. A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell 2006, 124:573-586.
13. Oertle T., Schwab M.E. Nogo and its partner. Trends Cell Biol. 2003, 13:187-194.
14. Oertle T., van der Haar M.E., Bandtlow C.E., Robeva A., Burfeind P., Buss A., Huber A.B., Simonen M., Schnell L., Brosamle C., Kaupmann K., Vallon R., Schwab M.E. Nogo-A inhibits neurite outgrowth and cell spreading with three discrete regions. J. Neurosci. 2003, 23:5393-5406.
15. Dodd D.A., Niederoes B., Bloechlinger S., Dupuis L., Loeffler J.P., Schwab M.E. NogoA, -B, -C are found in many different cell types. J. Biol. Chem. 2005, 280:12494-12502.
16. Fouad K., Dietz V., Schwab M.E. Improving axonal growth and functional recovery after experimental spinal cord injury by neutralizing myelin associated inhibitors. Brain Res. 2001, 36:204-212.
17. Emerick A.J., Neafsey E.J., Schwab M.E. Functional reorganization of the motor cortex in adult rats after cortical lesion and treatment with monoclonal antibody IN-1. J. Neurosci. 2003, 23:4826-4830.
18. McDonald C.L., Bandtlow C., Reindl M. Targeting the Nogo receptor complex in diseases of the central nervous system. Curr. Med. Chem. 2011, 18:234-244.
19. Quin H., Pu H.X., Li M., Ahmed S., Song J. Identification and structural mechanism for a novel interaction between a ubiquitin ligase WWP1 and Nogo-A, a key inhibitor for central nervous system regeneration. Biochemistry 2008, 47:13647-13658.
20. Wakana Y., Koyama S., Nakajima K., Hatsuzawa K., Nagahama M., Tani K., Hauri H.P., Melancon P., Tagaya M. Reticulon 3 is involved in membrane trafficking between the endoplasmic reticulum and Golgi. Biochem. Biophys. Res. Commun. 2005, 334:1198-1205.
21. Iwahashi J., Hamada N. Human reticulon 1-A and 1-B interact with a medium chain of the AP-2 adaptor complex. Cell. Mol. Biol. 2003, 49:467-471.
22. Steiner P., Kulangara K., Sarria J.C., Glauser L., Regazzi R., Hirling H. Reticulon 1-C/neuroendocrine-specific protein-C interacts with SNARE proteins. J. Neurochem. 2004, 89:569-580.
23. Fergani A., Dupuis L., Jokic N., Larmet Y., de Tapia M., Rene F., Loeffler J.P., Gonzales de Aguilar J.L. Reticulons as markers of neurological diseases: focus on amyotrophic lateral sclerosis. Neurodegener Dis 2005, 2:185-194.
24. Yan R., Shi Q., Zhou X. Reticulon proteins: emerging players in neurodegenerative diseases. Cell. Mol. Life Sci. 2006, 63:877-889.
25. Yokota T., Mishra M., Akatsu H., Tani Y., Miyauchi T., Yamamoto T., Kosaka K., Nagai Y., Sawada T., Heese K. Brain site-specific gene expression analysis in Alzheimer's disease patients. Eur. J. Clin. Invest. 2006, 36:820-830.
26. Murayama K.S., Kametani F., Saito S., Kume H., Akiyama H., Araki W. Reticulons RTN3 and RTN4-B/C interact with BACE1 and inhibit its ability to produce amyloid beta-protein. Eur. J. Neurosci. 2006, 24:1237-1244.
27. Shi Q., Prior M., He W., Tang X., Hu X., Yan R. Reduced amyloid deposition in mice overexpressing RTN3 is adversely affected by preformed dystrophic neuritis. J. Neurosci. 2009, 29:9163-9173.
28. Collas P., Poccia D. Membrane fusion events during nuclear envelope assembly. Subcell. Biochem. 2000, 34:273-302.
29. Anderson D.J., Hetzer M.W. Nuclear envelope formation by chromatin-mediated reorganization of the endoplasmic reticulum. Nat. Cell Biol. 2007, 9:1160-1166.
30. Dawson T.R., Lazarus M.D., Hetzer M.W., Wente S.R. ER membrane bending proteins are necessary for de novo nuclear pore formation. J. Cell Biol. 2009, 184:659-675.
31. Chadrin A., Hess B., San Roman M., Gatti X., Lombard B., Loew D., Barral Y., Palancade B., Doye V. Pom33, a novel transmembrane nucleoporin required for proper nuclear pore complex distribution. J. Cell Biol. 2010, 189:795-811.
32. Tabas I., Ron D. Integrating the mechanisms of apoptosis induced by endoplasmic reticulum stress. Nat. Cell Biol. 2011, 13:184-190.
33. Rodriguez D., Rojas-Rivera D., Hetz C. Integrating stress signals at the endoplasmic reticulum: the BCL-2 protein family rheostat. Biochim. Biophys. Acta 2010, 163:564-574.
34. Tagami S., Eguchi Y., Kinoshita M., Takeda M., Tsujimoto Y. A novel protein, RTN-XS, interacts with both Bcl-XL and Bcl-2 on endoplasmic reticulum and reduces their anti-apoptotic activity. Oncogene 2000, 19:5736-5746.
35. Li Q., Qi B., Oka K., Shimakage M., Yoshioka N., Inoue H., Hakura A., Kodama K., Stanbridge E.J., Yutsudo M. Link of a new type of apoptosis-inducing gene ASY/Nogo-B to human cancer. Oncogene 2001, 20:3929-3936.
36. Kuang E., Li Q., Xu X., Zou H., Qi T. ER stress triggers apoptosis induced by Nogo-B/ASY overexpression. Exp. Cell Res. 2006, 312:1983-1988.
37. Oertle T., Merkler D., Schwab M.E. Do cancer cells die because of Nogo-B?. Oncogene 2003, 22:1390-1399.
38. Schweigreiter R., Stasyk T., Contarini I., Frausher S., Oertle T., Klimashewski L., Huber L.A., Bandtlow C.E. Phosphorylation-regulated cleavage of the reticulon protein Nogo-B by caspase-7 at a noncanonical recognition site. Proteomics 2007, 7:4457-4467.
39. Di Sano F., Fazi B., Tufi R., Nardacci R., Piacentini M. Reticulon-1C acts as a molecular switch between endoplasmic reticulum stress and genotoxic cell death pathway in human neuroblastoma cells. J. Neurochem. 2007, 102:345-353.
40. 2+ levels favors plasma membrane surface exposure of calreticulin. Cell Death Differ. 2008, 15:274-282.
41. 2+ depletion triggers apoptotic signals for endoplasmic reticulum (ER) overload response induced by overexpressed reticulon 3 (RTN3/HAP). J. Cell. Physiol. 2005, 204:549-559.
42. Wan Q., Kuang E., Dong W., Zhou S., Xu H., Qi Y., Liu Y. Reticulon 3 mediates Bcl-2 accumulation in mitochondria in response to endoplasmic reticulum stress. Apoptosis 2007, 12:319-328.
43. Breckenridge D.G., Germain M., Mathai J.P., Nguyen M., Shore G.C. Regulation of apoptosis by endoplasmic reticulum pathways. Oncogene 2003, 22:8608-8618.
44. Oakes S.A., Scorrano L., Opferman J.T., Bassik M.C., Nishino M., Pozzan T., Korsmeyer S.J. Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:105-110.
45. Fazi B., Melino S., De Rubeis S., Bagni C., Paci M., Piacentini M., Di Sano F. Acetylation of RTN-1C regulates the induction of ER stress by the inhibition of HDAC activity in neuroectodermal tumors. Oncogene 2009, 28:3814-3824.
46. Mizushima N. Physiological functions of autophagy. Curr. Top. Microbiol. Immunol. 2009, 335:71-84.
47. Chen R., Jin R., Wu L., Ye X., Yang Y., Luo K., Wang W., Wu D., Ye X., Huang L., Huang T., Xiao G. Reticulon 3 attenuates the clearance of cytosolic prion aggregates via inhibiting autophagy. Autophagy 2011, 7:205-216.
48. 2+/calmodulin-dependent kinase contributes to the regulation of WIPI-1 at the onset of autophagy. Mol. Pharmacol. 2011, 80:1066-1075.
49. Fazi B., Biancolella M., Mehdawy B., Corazzari M., Minella D., Blandini F., Moreno S., Nardacci R., Nisticò R., Sepe S., Novelli G., Piacentini M., Di Sano F. Characterization of gene expression induced by RTN-1C in human neuroblastoma cells and in mouse brain. Neurobiol. Dis. 2010, 40:634-644.
50. Yang Y.S., Harel N.Y., Strittmatter S.M. Reticulon-4A (Nogo-A) redistributes protein disulfide isomerase to protect mice from SOD1-dependent amyotrophic lateral sclerosis. J. Neurosci. 2009, 29:13850-13859.
51. Hsu R., Woodroffe A., Lai W.S., Cook M.N., Mukai J., Dunning J.P., Swanson D.J., Roos J.L., Abecasis G.R., Karayiorgou M., Gogos M. Nogo Receptor 1 (RTN4R) as a candidate gene for schizophrenia: analysis using human and mouse genetic approaches. PLoS One 2007, 2:e1234.