The cell nucleus is a membrane-bound organelle found in eukaryotic cells. Eukaryotic cells usually have a single nucleus,but a few cell types,such as mammalian red blood cells,have no nuclei,and a few others including osteoclasts have many. The main structures making up the nucleus are the nuclear envelope,a double membrane that encloses the entire organelle and isolates its contents from the cellular cytoplasm;and the nuclear matrix,a network within the nucleus that adds mechanical support.
A nuclear pore is a channel as part of the nuclear pore complex (NPC),a large protein complex found in the nuclear envelope of eukaryotic cells. The nuclear envelope (NE) surrounds the cell nucleus containing DNA and facilitates the selective membrane transport of various molecules.
Telophase is the final stage in both meiosis and mitosis in a eukaryotic cell. During telophase,the effects of prophase and prometaphase are reversed. As chromosomes reach the cell poles,a nuclear envelope is re-assembled around each set of chromatids,the nucleoli reappear,and chromosomes begin to decondense back into the expanded chromatin that is present during interphase. The mitotic spindle is disassembled and remaining spindle microtubules are depolymerized. Telophase accounts for approximately 2% of the cell cycle's duration.
A nuclear localization signalorsequence (NLS) is an amino acid sequence that 'tags' a protein for import into the cell nucleus by nuclear transport. Typically,this signal consists of one or more short sequences of positively charged lysines or arginines exposed on the protein surface. Different nuclear localized proteins may share the same NLS. An NLS has the opposite function of a nuclear export signal (NES),which targets proteins out of the nucleus.
An alpha solenoid is a protein fold composed of repeating alpha helix subunits,commonly helix-turn-helix motifs,arranged in antiparallel fashion to form a superhelix. Alpha solenoids are known for their flexibility and plasticity. Like beta propellers,alpha solenoids are a form of solenoid protein domain commonly found in the proteins comprising the nuclear pore complex. They are also common in membrane coat proteins known as coatomers,such as clathrin,and in regulatory proteins that form extensive protein-protein interactions with their binding partners. Examples of alpha solenoid structures binding RNA and lipids have also been described.
Nuclear pore glycoprotein p62 is a protein complex associated with the nuclear envelope. The p62 protein remains associated with the nuclear pore complex-lamina fraction. p62 is synthesized as a soluble cytoplasmic precursor of 61 kDa followed by modification that involve addition of N-acetylglucosamine residues,followed by association with other complex proteins. In humans it is encoded by the NUP62 gene.
The nuclear envelope,also known as the nuclear membrane,is made up of two lipid bilayer membranes that in eukaryotic cells surround the nucleus,which encloses the genetic material.
Nucleoporins are a family of proteins which are the constituent building blocks of the nuclear pore complex (NPC). The nuclear pore complex is a massive structure embedded in the nuclear envelope at sites where the inner and outer nuclear membranes fuse,forming a gateway that regulates the flow of macromolecules between the cell nucleus and the cytoplasm. Nuclear pores enable the passive and facilitated transport of molecules across the nuclear envelope. Nucleoporins,a family of around 30 proteins,are the main components of the nuclear pore complex in eukaryotic cells. Nucleoporin 62 is the most abundant member of this family. Nucleoporins are able to transport molecules across the nuclear envelope at a very high rate. A single NPC is able to transport 60,000 protein molecules across the nuclear envelope every minute.
Nucleoporin 214 (Nup2014) is a protein that in humans is encoded by the NUP214 gene.
Nucleoporin 107 (Nup107) is a protein that in humans is encoded by the NUP107 gene.
Nuclear pore complex protein Nup133,or Nucleoporin Nup133,is a protein that in humans is encoded by the NUP133 gene.
Nucleoporin 85 (Nup85) is a protein that in humans is encoded by the NUP85 gene.
Nucleoporin 43 (Nup43) is a protein that in humans is encoded by the NUP43 gene.
Nucleoporin 37 (Nup37) is a protein that in humans is encoded by the NUP37 gene.
Nucleoporin 205 (Nup205) is a protein that in humans is encoded by the NUP205 gene.
Susan Wente is an American cell biologist and academic administrator currently serving as the 14th President of Wake Forest University. From 2014 to 2021 she was Provost and Vice Chancellor for Academic Affairs at Vanderbilt University. Between August 15,2019 and June 30,2020,she served as interim Chancellor at Vanderbilt.
Gene gating is a phenomenon by which transcriptionally active genes are brought next to nuclear pore complexes (NPCs) so that nascent transcripts can quickly form mature mRNA associated with export factors. Gene gating was first hypothesised by Günter Blobel in 1985. It has been shown to occur in Saccharomyces cerevisiae,Caenorhabditis elegans,Drosophila melanogaster as well as mammalian model systems.
David Fenyö is a Hungarian-Swedish-American computational biologist,physicist and businessman. He is currently professor in the Department of Biochemistry and Molecular Pharmacology at NYU Langone Medical Center. Fenyö's research focuses on the development of methods to identify,characterize and quantify proteins and in the integration of data from multiple modalities including mass spectrometry,sequencing and microscopy.
John D Aitchison is a Canadian American molecular cell biologist,systems cell biologist,and academic. He serves as a Principal Investigator at Seattle Children's Research Institute and Professor in the Department of Pediatrics,an Affiliate/Adjunct Professor in the Department of Biochemistry,at the University of Washington (UW). Serving as an Affiliate Professor at the Institute for Systems Biology (ISB),he is also an adjunct professor at University of Alberta (UAlberta).
AndréHoelz is a German-American structural cell biologist. Currently,he is the Mary and Charles Ferkel Professor of Chemistry and Biochemistry at the California Institute of Technology (Caltech) and an Investigator of the Howard Hughes Medical Institute (HHMI). He is best known for his research on the structure and function of the nuclear pore complex (NPC) and its role in nucleocytoplasmic transport.
