Welcome to Scribd, the world's digital library. Read, publish, and share books and documents. See more
Standard view
Full view
of .
Look up keyword
Like this
0 of .
Results for:
No results containing your search query
P. 1
Nuclear Pores and the Nuclear Pore Complex

Nuclear Pores and the Nuclear Pore Complex

Ratings: (0)|Views: 29 |Likes:
An essay for the 2011 Undergraduate Awards (Ireland) Competition by Sarah O'Brien. Originally submitted for TR071 at Trinity College, University of Dublin, with lecturer Dr Joe Carroll in the category of Life Sciences
An essay for the 2011 Undergraduate Awards (Ireland) Competition by Sarah O'Brien. Originally submitted for TR071 at Trinity College, University of Dublin, with lecturer Dr Joe Carroll in the category of Life Sciences

More info:

Published by: Undergraduate Awards on Aug 31, 2012
Copyright:Attribution Non-commercial


Read on Scribd mobile: iPhone, iPad and Android.
See more
See less


Nuclear Pores and the Nuclear Pore Complex
The nuclear pore is an opening that perforates the nuclear envelope (NE), the membranesurrounding the nucleus, at fused regions. Essentially the NE separates nuclear contentsfrom the rest of the cell, providing a protective barrier around the genetic materialcontained within. The NE is composed of two lipid bilayers, the outer nuclear membrane(ONM), on the cytoplasmic face and the inner nuclear membrane (INM), on the nuclear face [1]. The ONM is continuous with the endoplasmic reticulum (ER). Lipid bilayers areformed from the spontaneous association of membrane lipids. The space between the twolipid bilayers of the NE is called the lumen. The nuclear pore studs the NE and can befound at regions where the ONM and INM are fused forming an aqueous channel [1].The nuclear pore acts as a gateway between the nucleoplasm and the cytoplasm,facilitating exchange between the two. To facilitate this, the pore is filled by a proteinstructure called a nuclear pore complex (NPC). Transport through the NPC is selectiveand highly controlled and can occur actively or passively. Ions and small molecules candiffuse though the NPC but larger molecules >40kDa must but actively transported by the NPC [2]. The NPC has a life cycle; it is created, ages and dies with the cell. Certaindiseases have been linked to ageing and mutations of the NPC.
Structure of the Nuclear Pore Complex
The NPC is doughnut shaped and composed of a scaffold of eight (or multiples of eight)transmembrane proteins, which extend through the NE and surround a central channel.The central channel is ~45-50 nm in diameter [3]. There is much debate over theexistence of separate smaller channels around the central channel. If the eight-foldsymmetry of the NPC were to be conserved, these would be present in multiples of eight[4]. Two rings form above and below the scaffold, a cytoplasmic ring and a nuclear ring.These outer rings are composed of the yeast yNup84 complex (mNup107-160 complex inmetazoans) [5]. The scaffold is thought to be formed from the interactions of yNup170/157, yNup188 and yNup192 (mNup155, mNup188 and mNup205) [5]. There1
are eight filaments extending from each ring. The filaments on the cytoplasmic ring areuntied but the nuclear filaments are attached to a smaller ring and form a structure knownas a nuclear basket [6] (Figure 1). The distance through the fully formed NPC is thoughtto be ~200nm.The distribution of NPCs in intact NEs varies greatly between organisms, cell types andstage in the cell cycle, for example in budding yeast the region of the NE near the spindle pole bodies during mitosis has a higher density of NPCs than the rest of the NE [7].
oocytes are extremely densely packed having about 50 NPCs per squaremicrometer of NE [8] whereas human HeLa cells were found to have only 11 NPCs per square millimetre NE [9]. Distribution can be random or non-random. Non-randomdistribution has been observed in budding yeast and rat kidney cells [10]. However,2
. Shows structure of NPC [6].
despite these diversities, NPC structure has been evolutionarily conserved [11]. Thereare ~ 30 proteins in the NPC structure knowas nucleoporins or nups [12], and there arehomologs of nearly all nucleoporins between different organisms (Table 1).The completed NPC structure is composedof 400 – 1000 proteins, about 40 – 70mDa[12]. Yeast NPC is predicted to beassembled from 456 separate components[13]. Only certain types of proteins canfunction as nups. These are restricted to β- propellers, α-solenoids, phenylalanine – glycine (FG) nucleoporins, coiled – coiled proteins and transmembrane proteins [13,14]. Transmembrane nucleoporins help bindthe NPC to the NE. Transmembrane proteinscan be single pass, passing through themembrane only once, or multi pass, passingthrough multiple times. There are also core proteins, which make up the cytoplasmicand nucleoplasmic rings and linker proteins.In
the NPCscaffold is comprised of two proteincomplexes that anchor FG nucleoporinsthrough linker proteins [13]. These FGnucleoporins account for one-third of the total pore proteins [6]. The FG nucleoporins penetrate into the central channel from the scaffold, filling the channel and extending intothe nucleoplasm and cytoplasm. It is these FG nucleoporins that are responsible for 
MammalianS.cerevisiaeC. elegans
Nup35Nup53pNpp-19Nup37\\Nup43\C09G9.2Nup50Nup2pNpp-16Nup54Nup57pNpp-1Nup58/45Nup49pNpp-4Nup62Nsp1pNpp-11Nup75Nup85pNpp-2Nup88Nup82p\Nup93Nic96pNpp-13Nup96Nup145CpNpp-10Nup98Nup145NpNpp-10& Nup100p& Nup116pNup107Nup84pNpp-5Nup133Nup133pNpp-15Nup153Nup1pNpp-7& Nup2p& Nup60pNup155Nup157pNpp-8& Nup170pNup160Nup120pNpp-6Nup188Nup188p\Nup205Nup192pNpp-3Nup214Nup159pNpp-14Nup358\Npp-9Sec13RSec13pNpp-20Seh1SehpNpp-18Pom121\\Gp210\Npp-12Ndc1Ndc1pNpp-22TprMlp1pNpp-21& Mlp2pRAE1Gle2pNpp-17 ALADIN\\NLP1Nup42p\\Nup59p\\Nup116p\\Nup100p\\Pom134p\\Pom152p\ \ Indicates homolog is not knownSome proteins have more than one homologe.g. mammalian Nup155
Table 1.
Homologs of mammalian, S.cerevisiae and C. elegans nucleoporins [6]

You're Reading a Free Preview

/*********** DO NOT ALTER ANYTHING BELOW THIS LINE ! ************/ var s_code=s.t();if(s_code)document.write(s_code)//-->