Non-canonical ubiquitylation of the proneural protein Ngn2 occurs in both Xenopus embryos and mammalian cells

Biochemical and Biophysical Research Communications

Volumn 400, Issue 4, 2010, Pages 655-660

  McDowell, Gary S ^a   Kucerova, Romana ^a,b   Philpott, Anna ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b INSTITUTE OF MOLECULAR GENETICS   (Czech Republic)

Author keywords

BHLH; Cysteine; Neurogenesis; Ngn2; Ubiquitylation; Xenopus

Indexed keywords

CYSTEINE; NEUROGENIN 2;

ARTICLE; CARCINOMA CELL; IMMUNOPRECIPITATION; NERVE CELL DIFFERENTIATION; NERVOUS SYSTEM DEVELOPMENT; NEURULATION; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN METABOLISM; UBIQUITINATION; XENOPUS;

ANIMALS; EMBRYO, NONMAMMALIAN; FEMALE; MICE; NERVE TISSUE PROTEINS; PROTEASOME ENDOPEPTIDASE COMPLEX; UBIQUITINATION; XENOPUS LAEVIS; XENOPUS PROTEINS;

MAMMALIA;

EID: 77957270299     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.08.122     Document Type: Article

References (24)

1. Hershko A., Heller H., Elias S., Ciechanover A. Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J. Biol. Chem. 1983, 258:8206-8214.
2. Naujokat C., Saric T. Concise review: role and function of the ubiquitin-proteasome system in mammalian stem and progenitor cells. Stem Cells 2007, 25:2408-2418.
3. Kerscher O., Felberbaum R., Hochstrasser M. Modification of proteins by ubiquitin and ubiquitin-like proteins. Annu. Rev. Cell Dev. Biol. 2006, 22:159-180.
4. Glickman M.H., Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol. Rev. 2002, 82:373-428.
5. Breitschopf K., Bengal E., Ziv T., Admon A., Ciechanover A. A novel site for ubiquitination: the N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein. EMBO J. 1998, 17:5964-5973.
6. Ciechanover A., Ben-Saadon R. N-terminal ubiquitination: more protein substrates join in. Trends Cell Biol. 2004, 14:103-106.
7. Carvalho A.F., Pinto M.P., Grou C.P., Alencastre I.S., Fransen M., Sa-Miranda C., Azevedo J.E. Ubiquitination of mammalian Pex5p, the peroxisomal import receptor. J. Biol. Chem. 2007, 282:31267-31272.
8. Williams C., van den Berg M., Sprenger R.R., Distel B. A conserved cysteine is essential for Pex4p-dependent ubiquitination of the peroxisomal import receptor Pex5p. J. Biol. Chem. 2007, 282:22534-22543.
9. Cadwell K., Coscoy L. Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase. Science 2005, 309:127-130.
10. Cadwell K., Coscoy L. The specificities of Kaposi's sarcoma-associated herpesvirus-encoded E3 ubiquitin ligases are determined by the positions of lysine or cysteine residues within the intracytoplasmic domains of their targets. J. Virol. 2008, 82:4184-4189.
11. Tait S.W., de Vries E., Maas C., Keller A.M., D'Santos C.S., Borst J. Apoptosis induction by Bid requires unconventional ubiquitination and degradation of its N-terminal fragment. J. Cell. Biol. 2007, 179:1453-1466.
12. Ishikura S., Weissman A.M., Bonifacino J.S. Serine residues in the cytosolic tail of the T-cell antigen receptor α-chain mediate ubiquitination and ER-associated degradation of the unassembled protein. J. Biol. Chem. 2010, 285:23916-23924.
13. Kageyama R., Ohtsuka T., Shimojo H., Imayoshi I. Dynamic Notch signaling in neural progenitor cells and a revised view of lateral inhibition. Nat. Neurosci. 2008, 11:1247-1251.
14. Ma Q., Kintner C., Anderson D.J. Identification of neurogenin, a vertebrate neuronal determination gene. Cell 1996, 87:43-52.
15. Sun Y., Nadal-Vicens M., Misono S., Lin M.Z., Zubiaga A., Hua X., Fan G., Greenberg M.E. Neurogenin promotes neurogenesis and inhibits glial differentiation by independent mechanisms. Cell 2001, 104:365-376.
16. Vosper J.M., Fiore-Heriche C.S., Horan I., Wilson K., Wise H., Philpott A. Regulation of neurogenin stability by ubiquitin-mediated proteolysis. Biochem. J. 2007, 407:277-284.
17. Vosper J.M., McDowell G.S., Hindley C.J., Fiore-Heriche C.S., Kucerova R., Horan I., Philpott A. Ubiquitylation on canonical and non-canonical sites targets the transcription factor neurogenin for ubiquitin-mediated proteolysis. J. Biol. Chem. 2009, 284:15458-15468.
18. Farah M.H., Olson J.M., Sucic H.B., Hume R.I., Tapscott S.J., Turner D.L. Generation of neurons by transient expression of neural bHLH proteins in mammalian cells. Development 2000, 127:693-702.
19. Nieuwkoop P.D., Faber J. Normal Table of Xenopus laevis 1994, Garland Publishing, New York.
20. Rudnicki M.A., McBurney M.W. Cell culture methods and induction of differentiation of embryonal carcinoma cell lines. Teratocarcinomas and Embryonic Stem Cells: A Practical Approach 1987, 19-49. IRL Press. E.J. Robertson (Ed.).
21. Abramoff M.D., Magelhaes P.J., Ram S.J. Image processing with image. J. Biophoton. Int. 2004, 11:36-42.
22. Stewart D.P., Koss B., Bathina M., Perciavalle R.M., Bisanz K., Opferman J.T. Ubiquitin-independent degradation of antiapoptotic MCL-1. Mol. Cell Biol. 2010, 30:3099-3110.
23. Prakash S., Tian L., Ratliff K.S., Lehotzky R.E., Matouschek A. An unstructured initiation site is required for efficient proteasome-mediated degradation. Nat. Struct. Mol. Biol. 2004, 11:830-837.
24. Shabek N., Ciechanover A. Degradation of ubiquitin: the fate of the cellular reaper. Cell Cycle 2010, 9:523-530.