A Neuronal Isoform of the Aplysia CPEB Has Prion-Like Properties

Cell

Volumn 115, Issue 7, 2003, Pages 879-891

  Si, Kausik ^a   Lindquist, Susan ^b   Kandel, Eric R ^a  

^a New York State Psychiatric Institute ^*  (United States)

^b WHITEHEAD INSTITUTE FOR BIOMEDICAL RESEARCH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CYTOPLASMIC POLYADENYLATION ELEMENT BINDING PROTEIN; GLUTAMINE; MESSENGER RNA; PRION PROTEIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; APLYSIA; ARTICLE; CONTROLLED STUDY; MEMORY CONSOLIDATION; NONHUMAN; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FAMILY; PROTEIN FUNCTION; RNA TRANSLATION; SYNAPTIC TRANSMISSION; YEAST;

APLYSIA;

EID: 0348077417     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(03)01020-1     Document Type: Article

References (38)

1. Chernoff Y.O., Lindquist S.L., Ono B., Inge-Vechtomov S.G., Liebman S.W. Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor. Science. 268:1995;880-884.
2. Collinge J. Prion diseases of humans and animals. their causes and molecular basis Annu. Rev. Neurosci. 24:2001;519-550.
3. Coustou V., Deleu C., Saupe S., Begueret J. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc. Natl. Acad. Sci. USA. 94:1997;9773-9778.
4. Crist C.G., Nakayashiki T., Kurahashi H., Nakamura Y. a novel Sup35-prion variant propagated with non-Gln/Asn oligopeptide repeats in the absence of the chaperone protein Hsp104. Genes Cells. 8:2003;603-618. [PHI+].
5. de Moor C.H., Richter J.D. Cytoplasmic polyadenylation elements mediate masking and unmasking of cyclin B1 mRNA. EMBO J. 18:1999;2294-2303.
6. DePace A.H., Santoso A., Hillner P., Weissman J.S. A critical role for amino-terminal glutamine/asparagine repeats in the formation and propagation of a yeast prion. Cell. 93:1998;1241-1252.
7. Dichtl B., Blank D., Sadowski M., Hubner W., Weiser S., Keller W. Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II transcription termination. EMBO J. 21:2002;4125-4135.
8. Edskes H.K., Gray V.T., Wickner R.B. The [URE3] prion is an aggregated form of Ure2p that can be cured by overexpression of Ure2p fragments. Proc. Natl. Acad. Sci. USA. 96:1999;1498-1503.
9. Ferreira P.C., Ness F., Edwards S.R., Cox B.S., Tuite M.F. The elimination of the yeast [PSI+] prion by guanidine hydrochloride is the result of Hsp104 inactivation. Mol. Microbiol. 40:2001;1357-1369.
10. Glover J.R., Kowal A.S., Schirmer E.C., Patino M.M., Liu J.J., Lindquist S. Self-seeded fibers formed by Sup35, the protein determinant of [PSI+], a heritable prion-like factor of S. cerevisiae. Cell. 89:1997;811-819.
11. Hake L.E., Richter J.D. CPEB is a specificity factor that mediates cytoplasmic polyadenylation during Xenopus oocyte maturation. Cell. 79:1994;617-627.
12. Hake L.E., Mendez R., Richter J.D. Specificity of RNA binding by CPEB. requirement for RNA recognition motifs and a novel zinc finger Mol. Cell. Biol. 18:1998;685-693.
13. King C.Y., Tittmann P., Gross H., Gebert R., Aebi M., Wuthrich K. Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. Proc. Natl. Acad. Sci. USA. 94:1997;6618-6622.
14. Kushnirov V.V., Kochneva-Pervukhova N.V., Chechenova M.B., Frolova N.S., Ter-Avanesyan M.D. Prion properties of the Sup35 protein of yeast Pichia methanolica. EMBO J. 19:2000;324-331.
15. Li L., Lindquist S. Creating a protein-based element of inheritance. Science. 287:2000;661-664.
16. Lindquist S. Mad cows meet psi-chotic yeast. the expansion of the prion hypothesis Cell. 89:1997;495-498.
17. Liu J.J., Sondheimer N., Lindquist S.L. Changes in the middle region of Sup35 profoundly alter the nature of epigenetic inheritance for the yeast prion. Proc. Natl. Acad. Sci. USA. 99:2002;16446-16453. (Suppl 4).
18. Masison D.C., Wickner R.B. Prion-inducing domain of yeast Ure2p and protease resistance of Ure2p in prion-containing cells. Science. 270:1995;93-95.
19. Mendez R., Barnard D., Richter J.D. Differential mRNA translation and meiotic progression require Cdc2-mediated CPEB destruction. EMBO J. 21:2002;1833-1844.
20. Michelitsch M.D., Weissman J.S. A census of glutamine/asparagine-rich regions. implications for their conserved function and the prediction of novel prions Proc. Natl. Acad. Sci. USA. 97:2000;11910-11915.
21. Moriyama H., Edskes H.K., Wickner R.B. prion propagation in Saccharomyces cerevisiae. requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p Mol. Cell. Biol. 20:2000;8916-8922. [URE3].
22. Newnam G.P., Wegrzyn R.D., Lindquist S.L., Chernoff Y.O. Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Mol. Cell. Biol. 19:1999;1325-1333.
23. Osherovich L.Z., Weissman J.S. Multiple Gln/Asn-rich prion domains confer susceptibility to induction of the yeast [PSI(+)] prion. Cell. 106:2001;183-194.
24. Patino M.M., Liu J.J., Glover J.R., Lindquist S. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science. 273:1996;622-626.
25. Paushkin S.V., Kushnirov V.V., Smirnov V.N., Ter-Avanesyan M.D. In vitro propagation of the prion-like state of yeast Sup35 protein. Science. 277:1997;381-383.
26. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. USA. 95:1998;13363-13383.
27. Roberts B.T., Wickner R.B. Heritable activity. a prion that propagates by covalent autoactivation Genes Dev. 17:2003;2083-2087.
28. Shatkin A.J., Manley J.L. The ends of the affair. capping and polyadenylation Nat. Struct. Biol. 7:2000;838-842.
29. Si K., Giustetto M., Etkin A., Hsu R., Janisiewicz A.M., Miniaci M.C., Kim J.H., Zhu H., Kandel E.R. A neuronal isoform of CPEB regulates local protein synthesis and stabilizes synapse-specific long-term facilitation in aplysia. Cell. 115:2003;893-904. , this issue.
30. Sondheimer N., Lindquist S. Rnq1. an epigenetic modifier of protein function in yeast Mol. Cell. 5:2000;163-172.
31. Sparrer H.E., Santoso A., Szoka F.C. Jr., Weissman J.S. Evidence for the prion hypothesis. induction of the yeast [PSI+] factor by in vitro-converted Sup35 protein Science. 289:2000;595-599.
32. Stebbins-Boaz B., Hake L.E., Richter J.D. CPEB controls the cytoplasmic polyadenylation of cyclin, Cdk2 and c-mos mRNAs and is necessary for oocyte maturation in Xenopus. EMBO J. 15:1996;2582-2592.
33. Stumpf G., Domdey H. Dependence of yeast pre-mRNA 3′-end processing on CFT1. a sequence homolog of the mammalian AAUAAA binding factor Science. 274:1996;1517-1520.
34. Theis M., Si K., Kandel E.R. Two previously undescribed members of the mouse CPEB family of genes and their inducible expression in the principal cell layers of the hippocampus. Proc. Natl. Acad. Sci. USA. 100:2003;9602-9607.
35. True H.L., Lindquist S.L. A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature. 407:2000;477-483.
36. Tuite M.F. Yeast prions and their prion-forming domain. Cell. 100:2000;289-292.
37. Wickner R.B. as an altered URE2 protein. evidence for a prion analog in Saccharomyces cerevisiae Science. 264:1994;566-569. [URE3].
38. Wickner R.B., Masison D.C. Evidence for two prions in yeast. [URE3] and Curr. Top. Microbiol. Immunol. 207:1996;147-160. [PSI].