SET7/9 mediated methylation of non-histone proteins in mammalian cells.
Lysine methylation has emerged as a major posttranslational modification for histones in eukaryotes. Crosstalk between lysine methylation and other posttranslational modifications is crucial for transcriptional gene regulation and epigenetic inheritance. In addition to histones, several other cellular proteins including transcription factors, tumor suppressor and membrane-associated receptors are subject to lysine methylation. SET7/9 plays a prominent role in lysine methylation of histone and non-histone proteins. Recent reports have suggested a new mechanism of epigenetic gene regulation via SET7/9 modulated DNMT1 methylation. In this mechanism, SET7/9 may methylate DNMT1 leading to proteasome mediated protein degradation, and antagonist lysine specific demethylase (LSD), may prevent this degradation by removing the methyl mark. Thus a fine-tuning and balance between cellular SET7/9 and LSD interaction with DNMT1 may be means for epigenetic gene regulation.
Pradhan
Sriharsa
S
New England Biolabs Inc, Ipswich, MA, USA. pradhan@neb.com
Chin
Hang Gyeong
HG
Estève
Pierre-Olivier
PO
Jacobsen
Steven E
SE
D000818:Animals; D000076123:DNA (Cytosine-5-)-Methyltransferase 1; D004248:DNA (Cytosine-5-)-Methyltransferases / Q000378:metabolism; D044127:Epigenesis, Genetic; D005786:Gene Expression Regulation; D011495:Histone-Lysine N-Methyltransferase / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D008322:Mammals / Q000235:genetics*; D008745:Methylation; D051379:Mice; D008957:Models, Genetic; D046988:Proteasome Endopeptidase Complex / Q000502:physiology
D000076123:DNA (Cytosine-5-)-Methyltransferase 1; D004248:DNA (Cytosine-5-)-Methyltransferases; C000619380:DNMT1 protein, human; C000619381:Dnmt1 protein, mouse; D011495:Histone-Lysine N-Methyltransferase; C540312:SETD7 protein, human; D046988:Proteasome Endopeptidase Complex; D008239:Lysine
Cell. 2007 Feb 23;128(4):693-705
17320507
Diabetes. 2009 Jan;58(1):185-93
18984737
Cell. 2002 Oct 4;111(1):105-15
12372304
Nature. 2005 Jan 27;433(7024):434-8
15647753
Ann N Y Acad Sci. 2008 Sep;1138:366-75
18837912
Mol Endocrinol. 2009 Apr;23(4):425-33
19164444
J Biol Chem. 2008 Sep 26;283(39):26771-81
18650421
Cell. 1997 Aug 22;90(4):595-606
9288740
J Biol Chem. 2008 Dec 19;283(51):35561-8
18957409
Nature. 2003 Feb 6;421(6923):652-6
12540855
Cell. 1992 Jun 12;69(6):915-26
1606615
Mol Cell. 2004 Apr 23;14(2):175-82
15099517
Microbiol Mol Biol Rev. 2000 Jun;64(2):435-59
10839822
Nature. 2007 Sep 6;449(7158):105-8
17805299
Mol Cell. 2003 Jul;12(1):177-85
12887903
Nature. 2006 Jul 6;442(7098):96-9
16728974
J Am Chem Soc. 2008 Mar 26;130(12):3806-13
18311969
Nat Struct Mol Biol. 2006 Feb;13(2):140-6
16415881
Mol Cell. 2008 May 9;30(3):336-47
18471979
Nature. 2006 Jul 6;442(7098):100-3
16728977
Nature. 2004 Nov 18;432(7015):353-60
15525938
Nat Genet. 2009 Jan;41(1):125-9
19098913
Proc Natl Acad Sci U S A. 2009 Mar 31;106(13):5076-81
19282482
Mol Cell. 2001 Dec;8(6):1207-17
11779497
EMBO J. 1994 Aug 15;13(16):3822-31
7915232
Mol Cell Biol. 1993 Oct;13(10):6357-66
8413234
Nature. 2000 Aug 10;406(6796):593-9
10949293
Mol Cell Biol. 2007 Oct;27(19):6756-69
17646389
Nat Struct Biol. 2003 Jul;10(7):545-52
12819771
Curr Opin Genet Dev. 2008 Apr;18(2):169-74
18329871
Mol Cell Biol. 2005 Jun;25(11):4727-41
15899874
Mech Dev. 1995 Aug;52(2-3):209-23
8541210
Mol Cell. 2008 Feb 15;29(3):392-400
18280244
Science. 2006 May 5;312(5774):748-51
16601153
Nature. 2006 Jul 6;442(7098):86-90
16728976