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PMID: 17906672 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

The inner nuclear envelope as a transcription factor resting place.

EMBO reports ·Vol. 8 ·No. 10 ·2007-10-00 ·Pages 914-9

Heessen S, Fornerod M

Abstract

Just as people head to the beaches for a well-deserved rest, accumulating evidence suggests that transcription factors take similar 'vacations' at the nuclear envelope. Recent studies indicate that the periphery of the nucleus provides a platform for sequestering transcription factors away from chromatin. Several transcriptional regulators, operating in different signal-transduction pathways, have been found to interact physically with components of the inner nuclear membrane. In general, this association seems to restrict access to their target genes and limit their transactivation or transrepression abilities. The mechanisms of inner nuclear membrane association are diverse, and include regulated associations with the nuclear lamina and integral membrane proteins. Together, these findings indicate that the inside of the nuclear envelope functions as a resting place for transcription factors and suggest a more direct role for the nuclear envelope in gene regulation than previously anticipated.

MeSH Terms
Animals Humans Lamins/metabolism Models, Biological Nuclear Envelope/metabolism Nuclear Lamina/metabolism Nuclear Proteins/metabolism Signal Transduction Transcription Factors/metabolism
Chemicals
Lamins Nuclear Proteins Transcription Factors
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Heessen Stijn
Department of Tumour Biology, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.
Fornerod Maarten
References (40)
40 references, click to expand
  1. Smad transcription factors.
    Genes Dev. 2005 Dec 1;19(23):2783-810 PMID: 16322555
  2. Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation.
    Cell. 1993 Jul 2;73(7):1267-79 PMID: 8324822
  3. Amino acid signaling in yeast: casein kinase I and the Ssy5 endoprotease are key determinants of endoproteolytic activation of the membrane-bound Stp1 transcription factor.
    Mol Cell Biol. 2004 Nov;24(22):9771-85 PMID: 15509782
  4. A-type lamins regulate retinoblastoma protein function by promoting subnuclear localization and preventing proteasomal degradation.
    Proc Natl Acad Sci U S A. 2004 Jun 29;101(26):9677-82 PMID: 15210943
  5. Regulation of peroxisome proliferator-activated receptor gamma expression by adipocyte differentiation and determination factor 1/sterol regulatory element binding protein 1: implications for adipocyte differentiation and metabolism.
    Mol Cell Biol. 1999 Aug;19(8):5495-503 PMID: 10409739
  6. Stp1p, Stp2p and Abf1p are involved in regulation of expression of the amino acid transporter gene BAP3 of Saccharomyces cerevisiae.
    Nucleic Acids Res. 2000 Feb 15;28(4):974-81 PMID: 10648791
  7. Inner nuclear membrane proteins Asi1, Asi2, and Asi3 function in concert to maintain the latent properties of transcription factors Stp1 and Stp2.
    J Biol Chem. 2007 Jan 5;282(1):594-605 PMID: 17085444
  8. Suppressors of ssy1 and ptr3 null mutations define novel amino acid sensor-independent genes in Saccharomyces cerevisiae.
    Genetics. 2001 Jul;158(3):973-88 PMID: 11454748
  9. The nuclear membrane proteome: extending the envelope.
    Trends Biochem Sci. 2005 Oct;30(10):551-8 PMID: 16125387
  10. Emerin binding to Btf, a death-promoting transcriptional repressor, is disrupted by a missense mutation that causes Emery-Dreifuss muscular dystrophy.
    Eur J Biochem. 2004 Mar;271(5):1035-45 PMID: 15009215
  11. What MAN1 does to the Smads. TGFbeta/BMP signaling and the nuclear envelope.
    FEBS J. 2007 Mar;274(6):1374-82 PMID: 17489095
  12. Dissociation of Oct-1 from the nuclear peripheral structure induces the cellular aging-associated collagenase gene expression.
    Mol Biol Cell. 1997 Dec;8(12):2407-19 PMID: 9398664
  13. Regulation of transcription factor latency by receptor-activated proteolysis.
    Genes Dev. 2006 Jun 15;20(12):1563-8 PMID: 16778074
  14. Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro.
    J Biol Chem. 2003 Feb 28;278(9):6969-75 PMID: 12493765
  15. The nuclear lamina comes of age.
    Nat Rev Mol Cell Biol. 2005 Jan;6(1):21-31 PMID: 15688064
  16. The nuclear envelope and the architecture of the nuclear periphery.
    J Cell Biol. 1981 Dec;91(3 Pt 2):39s-50s PMID: 7033243
  17. The nuclear envelope protein MAN1 regulates TGFbeta signaling and vasculogenesis in the embryonic yolk sac.
    Development. 2007 Apr;134(7):1385-95 PMID: 17329363
  18. MAN1, an inner nuclear membrane protein that shares the LEM domain with lamina-associated polypeptide 2 and emerin.
    J Biol Chem. 2000 Feb 18;275(7):4840-7 PMID: 10671519
  19. Direct binding of nuclear membrane protein MAN1 to emerin in vitro and two modes of binding to barrier-to-autointegration factor.
    J Biol Chem. 2005 Apr 8;280(14):13863-70 PMID: 15681850
  20. XMAN1, an inner nuclear membrane protein, antagonizes BMP signaling by interacting with Smad1 in Xenopus embryos.
    Development. 2003 May;130(9):1783-94 PMID: 12642484
  21. MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-beta signaling.
    Hum Mol Genet. 2005 Feb 1;14(3):437-45 PMID: 15601644
  22. Nucleoplasmic LAP2alpha-lamin A complexes are required to maintain a proliferative state in human fibroblasts.
    J Cell Biol. 2007 Jan 15;176(2):163-72 PMID: 17227891
  23. Man1, an inner nuclear membrane protein, regulates vascular remodeling by modulating transforming growth factor beta signaling.
    Development. 2006 Oct;133(19):3919-28 PMID: 16943282
  24. A mechanism of AP-1 suppression through interaction of c-Fos with lamin A/C.
    Genes Dev. 2006 Feb 1;20(3):307-20 PMID: 16452503
  25. The integral inner nuclear membrane protein MAN1 physically interacts with the R-Smad proteins to repress signaling by the transforming growth factor-{beta} superfamily of cytokines.
    J Biol Chem. 2005 Apr 22;280(16):15992-6001 PMID: 15647271
  26. Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein.
    Mol Biol Cell. 2002 Dec;13(12):4401-13 PMID: 12475961
  27. Alteration of nuclear lamin organization inhibits RNA polymerase II-dependent transcription.
    J Cell Biol. 2002 Feb 18;156(4):603-8 PMID: 11854306
  28. Inner nuclear membrane and regulation of Smad-mediated signaling.
    Biochim Biophys Acta. 2006 May-Jun;1761(5-6):626-31 PMID: 16574476
  29. Nuclear membrane proteins with potential disease links found by subtractive proteomics.
    Science. 2003 Sep 5;301(5638):1380-2 PMID: 12958361
  30. Asi1 is an inner nuclear membrane protein that restricts promoter access of two latent transcription factors.
    J Cell Biol. 2006 Jun 5;173(5):695-707 PMID: 16735580
  31. The inner nuclear membrane protein emerin regulates beta-catenin activity by restricting its accumulation in the nucleus.
    EMBO J. 2006 Jul 26;25(14):3275-85 PMID: 16858403
  32. Altered pre-lamin A processing is a common mechanism leading to lipodystrophy.
    Hum Mol Genet. 2005 Jun 1;14(11):1489-502 PMID: 15843404
  33. Receptor-mediated endoproteolytic activation of two transcription factors in yeast.
    Genes Dev. 2002 Dec 15;16(24):3158-72 PMID: 12502738
  34. Btf, a novel death-promoting transcriptional repressor that interacts with Bcl-2-related proteins.
    Mol Cell Biol. 1999 Jun;19(6):4390-404 PMID: 10330179
  35. Nuclear lamins: their structure, assembly, and interactions.
    J Struct Biol. 1998;122(1-2):42-66 PMID: 9724605
  36. Transcriptional regulation of the Saccharomyces cerevisiae amino acid permease gene BAP2.
    Mol Gen Genet. 2001 Jan;264(5):613-22 PMID: 11212916
  37. Nuclear membrane protein LAP2beta mediates transcriptional repression alone and together with its binding partner GCL (germ-cell-less).
    J Cell Sci. 2001 Sep;114(Pt 18):3297-307 PMID: 11591818
  38. Lamin A/C speckles mediate spatial organization of splicing factor compartments and RNA polymerase II transcription.
    J Cell Biol. 2002 Dec 9;159(5):783-93 PMID: 12473687
  39. Nuclear envelope proteomics: novel integral membrane proteins of the inner nuclear membrane.
    Proc Natl Acad Sci U S A. 2001 Oct 9;98(21):11943-8 PMID: 11593002
  40. The nuclear envelope and transcriptional control.
    Nat Rev Genet. 2007 Jul;8(7):507-17 PMID: 17549064
Article Info
Journal
EMBO reports
Abbr.
EMBO Rep
ISSN
1469-221X
Published
2007-10-00
Pages
914-9
Language
English
Region
England
NLM ID
100963049
PMCID
PMC2002563
Subset
IM
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