Nuclear membrane

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Nuclear membrane
Diagram human cell nucleus.svg
Human cell nucleus
Identifiers
TH H1.00.01.2.01001
FMA 63888
Anatomical terminology

A nuclear membrane, also known as the nuclear envelope,[1][a] is the lipid bilayer membrane which surrounds the genetic material and nucleolus in eukaryotic cells.

The nuclear membrane consists of two lipid bilayers—the inner nuclear membrane, and the outer nuclear membrane. The space between the membranes is called the perinuclear space, a region contiguous with the lumen (inside) of the endoplasmic reticulum. It is usually about 20–40 nm wide.[4][5] The nuclear membrane also has many small holes called nuclear pores that allow material to move in and out of the nucleus.

Outer membrane[edit]

The outer nuclear membrane also shares a common border with the endoplasmic reticulum.[6] While it is physically linked, the outer nuclear membrane contains proteins found in far higher concentrations than the endoplasmic reticulum.[7] All 4 Nesprin proteins present in mammals are expressed in the outer nuclear membrane.[8] Nesprin proteins connect cytoskeletal filaments to the nucleoskeleton.[9] Nesprin-mediated connections to the cytoskeleton contribute to nuclear positioning and to the cell’s mechanosensory function.[10] KASH-domain proteins of Nesprin-1 and -2 are part of a LINC complex (Linker of Nucleoskeleton and Cytoskeleton) and can bind directly to cystoskeletal components, such as actin filaments, or can bind to proteins in the luminal domain of the nuclear membrane.[11] Nesprin-3 and-4 may play a role in unloading enormous cargo; Nesprin-3 proteins bind plectin and link the nuclear envelope to cytoplasmic intermediate filaments.[12] Nesprin-4 proteins bind the plus end directed motor kinesin-1.[13] The outer nuclear membrane is also involved in development, as it fuses with the inner nuclear membrane to form nuclear pores.[14]

Inner membrane[edit]

The inner nuclear membrane encloses the nucleoplasm, and is covered by the nuclear lamina, a mesh of intermediate filaments which stabilizes the nuclear membrane as well as being involved in chromatin function and entire expression.[7] It is connected to the outer membrane by nuclear pores which penetrate the membranes. While the two membranes and the endoplasmic reticulum are linked, proteins embedded in the membranes tend to stay put rather than dispersing across the continuum.[15] It is lined with a fiber network called as nuclear lamina which is 10-40 nm thick and provide strength.

Nuclear pores[edit]

The nuclear membrane is punctured by thousands of nuclear pore complexes—large hollow proteins about 100 nm across, with an inner channel about 40 nm wide.[7] They link the inner and outer nuclear membranes.

Cell division[edit]

During the G2 phase of interphase, the nuclear membrane increases its surface area and doubles its number of nuclear pore complexes.[7] In eukaryotes, such as yeast, which undergo closed mitosis, the nuclear membrane stays intact during cell division. The spindle fibers either form within the membrane, or penetrate it without tearing it apart.[7] In other eukaryotes (animals as well as plants), the nuclear membrane must break down during the prometaphase state of mitosis to allow the mitotic spindle fibers to access the chromosomes inside. The breakdown and reformation processes are not well understood.

Breakdown[edit]

In mammals, the nuclear membrane can break down within minutes, following a set of steps during the early stages of mitosis. First, M-Cdk's phosphorylate nucleoporin polypeptides and they are selectively removed from the nuclear pore complexes. After that, the rest of the nuclear pore complexes break apart simultaneously. Biochemical evidence suggests that the nuclear pore complexes disassemble into stable pieces rather than disintegrating into small polypeptide fragments.[7] M-Cdk's also phosphorylate elements of the nuclear lamina (the framework that supports the envelope) leading to the dis-assembly of the lamina and hence the envelope membranes into small vesicles.[16] Electron and fluorescence microscopy has given strong evidence that the nuclear membrane is absorbed by the endoplasmic reticulum—nuclear proteins not normally found in the endoplasmic reticulum show up during mitosis.[7]

Reformation[edit]

Exactly how the nuclear membrane reforms during telophase of mitosis is debated. Two theories exist[7]

  • Vesicle fusion—where vesicles of nuclear membrane fuse together to rebuild the nuclear membrane
  • Reshaping of the endoplasmic reticulum—where the parts of the endoplasmic reticulum containing the absorbed nuclear membrane envelop the nuclear space, reforming a closed membrane.

Origin of the nuclear membrane[edit]

A study of the comparative genomics, evolution and origins of the nuclear membrane led to the proposal that the nucleus emerged in the primitive eukaryotic ancestor (the “prekaryote”), and was triggered by the archaeo-bacterial symbiosis.[17] Several ideas have been proposed for the evolutionary origin of the nuclear membrane.[18] These ideas include the invagination of the plasma membrane in a prokaryote ancestor, or the formation of a genuine new membrane system following the establishment of proto-mitochondria in the archael host. The adaptive function of the nuclear membrane may have been to serve as a barrier to protect the genome from reactive oxygen species (ROS) produced by the cells' pre-mitochondria.[19][20]

Membrane rupture during interphase[edit]

In addition to the breakdown of the nuclear nuclear membrane during the prometaphase stage of mitosis, the nuclear membrane also ruptures in migrating mammalian cells during the interphase stage of the cell cycle.[21] This transient rupture is likely caused by nuclear deformation. The rupture is rapidly repaired by a process dependent on “endosomal sorting complexes required for transport” (ESCRT).[21] During nuclear membrane rupture events, DNA double-strand breaks occur. Thus the survival of cells migrating through confined environments appears to depend on efficient nuclear envelope and DNA repair machineries.

Notes[edit]

  1. ^ Less used names include nucleolemma[2] and karyotheca.[3]

References[edit]

  1. ^ Georgia State University. "Cell Nucleus and Nuclear Envelope". gsu.edu. 
  2. ^ "Nuclear membrane". Biology Dictionary. Biology Online. Retrieved 7 December 2012. 
  3. ^ "nuclear membrane". Merriam Webster. Retrieved 7 December 2012. 
  4. ^ "Perinuclear space". Dictionary. Biology Online. Retrieved 7 December 2012. 
  5. ^ Berrios, Miguel, ed. (1998). Nuclear structure and function. San Diego: Academic Press. p. 4. ISBN 9780125641555. 
  6. ^ "Chloride channels in the Nuclear membrane" (PDF). Harvard.edu. Retrieved 7 December 2012. 
  7. ^ a b c d e f g h Hetzer, Mertin (February 3, 2010). "The Nuclear Envelope". Cold Spring Harbor Perspectives in Biology. 2 (3): a000539. doi:10.1101/cshperspect.a000539. PMC 2829960Freely accessible. PMID 20300205. 
  8. ^ Wilson, Katherine L.; Berk, Jason M. (2010-06-15). "The nuclear envelope at a glance". J Cell Sci. 123 (12): 1973–1978. doi:10.1242/jcs.019042. ISSN 0021-9533. PMC 2880010Freely accessible. PMID 20519579. 
  9. ^ Burke, Brian; Roux, Kyle J. (2009-11-01). "Nuclei take a position: managing nuclear location". Developmental Cell. 17 (5): 587–597. doi:10.1016/j.devcel.2009.10.018. ISSN 1878-1551. PMID 19922864. 
  10. ^ Uzer, Gunes; Thompson, William R.; Sen, Buer; Xie, Zhihui; Yen, Sherwin S.; Miller, Sean; Bas, Guniz; Styner, Maya; Rubin, Clinton T. (2015-06-01). "Cell Mechanosensitivity to Extremely Low-Magnitude Signals Is Enabled by a LINCed Nucleus". STEM CELLS. 33 (6): 2063–2076. doi:10.1002/stem.2004. ISSN 1066-5099. PMC 4458857Freely accessible. PMID 25787126. 
  11. ^ Crisp, Melissa; Liu, Qian; Roux, Kyle; Rattner, J. B.; Shanahan, Catherine; Burke, Brian; Stahl, Phillip D.; Hodzic, Didier (2006-01-02). "Coupling of the nucleus and cytoplasm: role of the LINC complex". The Journal of Cell Biology. 172 (1): 41–53. doi:10.1083/jcb.200509124. ISSN 0021-9525. PMC 2063530Freely accessible. PMID 16380439. 
  12. ^ Wilhelmsen, Kevin; Litjens, Sandy H. M.; Kuikman, Ingrid; Tshimbalanga, Ntambua; Janssen, Hans; van den Bout, Iman; Raymond, Karine; Sonnenberg, Arnoud (2005-12-05). "Nesprin-3, a novel outer nuclear membrane protein, associates with the cytoskeletal linker protein plectin". The Journal of Cell Biology. 171 (5): 799–810. doi:10.1083/jcb.200506083. ISSN 0021-9525. PMC 2171291Freely accessible. PMID 16330710. 
  13. ^ Roux, Kyle J.; Crisp, Melissa L.; Liu, Qian; Kim, Daein; Kozlov, Serguei; Stewart, Colin L.; Burke, Brian (2009-02-17). "Nesprin 4 is an outer nuclear membrane protein that can induce kinesin-mediated cell polarization". Proceedings of the National Academy of Sciences of the United States of America. 106 (7): 2194–2199. doi:10.1073/pnas.0808602106. ISSN 1091-6490. PMC 2650131Freely accessible. PMID 19164528. 
  14. ^ Fichtman, Boris; Ramos, Corinne; Rasala, Beth; Harel, Amnon; Forbes, Douglass J. (2010-12-01). "Inner/Outer Nuclear Membrane Fusion in Nuclear Pore Assembly". Molecular Biology of the Cell. 21 (23): 4197–4211. doi:10.1091/mbc.E10-04-0309. ISSN 1059-1524. PMC 2993748Freely accessible. PMID 20926687. 
  15. ^ "The inner nuclear membrane: simple, or very complex?". The EMBO Journal. 20 (12): 2989–2994. April 19, 2001. doi:10.1093/emboj/20.12.2989. PMC 150211Freely accessible. PMID 11406575. Retrieved 7 December 2012. 
  16. ^ Alberts (et al) (2008). "Chapter 17: The Cell Cycle". Molecular Biology of The Cell (5th ed.). New York: Garland Science. pp. 1079–1080. ISBN 978-0-8153-4106-2. 
  17. ^ Mans BJ, Anantharaman V, Aravind L, Koonin EV (2004). "Comparative genomics, evolution and origins of the nuclear envelope and nuclear pore complex". Cell Cycle. 3 (12): 1612–37. doi:10.4161/cc.3.12.1345. PMID 15611647. 
  18. ^ Martin W (2005). "Archaebacteria (Archaea) and the origin of the eukaryotic nucleus". Curr. Opin. Microbiol. 8 (6): 630–7. doi:10.1016/j.mib.2005.10.004. PMID 16242992. 
  19. ^ Speijer D (2015). "Birth of the eukaryotes by a set of reactive innovations: New insights force us to relinquish gradual models". BioEssays. 37 (12): 1268–76. doi:10.1002/bies.201500107. PMID 26577075. 
  20. ^ Bernstein H, Bernstein C. Sexual communication in archaea, the precursor to meiosis. pp. 103-117 in Biocommunication of Archaea (Guenther Witzany, ed.) 2017. Springer International Publishing ISBN 978-3-319-65535-2 DOI 10.1007/978-3-319-65536-9
  21. ^ a b Raab M, Gentili M, de Belly H, Thiam HR, Vargas P, Jimenez AJ, Lautenschlaeger F, Voituriez R, Lennon-Duménil AM, Manel N, Piel M (2016). "ESCRT III repairs nuclear envelope ruptures during cell migration to limit DNA damage and cell death". Science. 352 (6283): 359–62. doi:10.1126/science.aad7611. PMID 27013426. 

External links[edit]