Results 11 to 20 of about 315,665 (286)

Protein quality control at the inner nuclear membrane [PDF]

Nature, 2014
The nuclear envelope is a double membrane that separates the nucleus from the cytoplasm. The inner nuclear membrane (INM) functions in essential nuclear processes including chromatin organization and regulation of gene expression. The outer nuclear membrane is continuous with the endoplasmic reticulum and is the site of membrane protein synthesis ...
Khmelinskii, Anton, Blaszczak, Ewa, Pantazopoulou, Marina, Fischer, Bernd, Omnus, Deike J, Le Dez, Gaëlle, Brossard, Audrey, Gunnarsson, Alexander, Barry, Joseph D, Meurer, Matthias, Kirrmaier, Daniel, Boone, Charles, Huber, Wolfgang, Rabut, Gwenaël, Ljungdahl, Per O, Knop, Michael   +15 more
openaire   +5 more sources

Structural Basis of Vesicle Formation at the Inner Nuclear Membrane [PDF]

Cell, 2015
Vesicular nucleo-cytoplasmic transport is becoming recognized as a general cellular mechanism for translocation of large cargoes across the nuclear envelope. Cargo is recruited, enveloped at the inner nuclear membrane (INM), and delivered by membrane fusion at the outer nuclear membrane.
Hagen, Christoph, Dent, Kyle C., Zeev-Ben-Mordehai, Tzviya, Grange, Michael, Bosse, Jens B., Whittle, Cathy, Klupp, Barbara G., Siebert, C. Alistair, Vasishtan, Daven, Baeuerlein, Felix J. B., Cheleski, Juliana, Werner, Stephan, Guttmann, Peter, Rehbein, Stefan, Henzler, Katja, Demmerle, Justin, Adler, Barbara, Koszinowski, Ulrich, Schermelleh, Lothar, Schneider, Gerd, Enquist, Lynn W., Plitzko, Juergen M., Mettenleiter, Thomas C., Gruenewald, Kay   +23 more
openaire   +7 more sources

Reprogrammed lipid metabolism protects inner nuclear membrane against unsaturated fat. [PDF]

Dev Cell, 2021
The cell nucleus is surrounded by a double membrane. The lipid packing and viscosity of membranes is critical for their function and is tightly controlled by lipid saturation. Circuits regulating the lipid saturation of the outer nuclear membrane (ONM) and contiguous endoplasmic reticulum (ER) are known.
Romanauska A, Köhler A.
europepmc   +5 more sources

Single-point single-molecule FRAP distinguishes inner and outer nuclear membrane protein distribution

Nature Communications, 2016
Nuclear envelope transmembrane proteins (NETs) can reside in the outer or inner nuclear membrane, but distinguishing which membrane they reside in, and their translocation rate, is technically challenging.
Krishna C Mudumbi, Eric C Schirmer, Weidong Yang   +2 more
doaj   +2 more sources

Compartmentalized Synthesis of Triacylglycerol at the Inner Nuclear Membrane Regulates Nuclear Organization. [PDF]

Dev Cell, 2019
Cells dynamically adjust organelle organization in response to growth and environmental cues. This requires regulation of synthesis of phospholipids, the building blocks of organelle membranes, or remodeling of their fatty-acyl (FA) composition. FAs are also the main components of triacyglycerols (TGs), which enable energy storage in lipid droplets ...
Barbosa AD, Lim K, Mari M, Edgar JR, Gal L, Sterk P, Jenkins BJ, Koulman A, Savage DB, Schuldiner M, Reggiori F, Wigge PA, Siniossoglou S.   +12 more
europepmc   +7 more sources

SUMOylation at the inner nuclear membrane facilitates nuclear envelope biogenesis during mitosis. [PDF]

J Cell Biol, 2023
As eukaryotic cells progress through cell division, the nuclear envelope (NE) membrane must expand to accommodate the formation of progeny nuclei. In Saccharomyces cerevisiae, closed mitosis allows visualization of NE biogenesis during mitosis. During this period, the SUMO E3 ligase Siz2 binds the inner nuclear membrane (INM) and initiates a wave of ...
Saik NO, Ptak C, Rehman S, Aitchison JD, Montpetit B, Wozniak RW.   +5 more
europepmc   +5 more sources

The Diverse Cellular Functions of Inner Nuclear Membrane Proteins. [PDF]

Cold Spring Harb Perspect Biol, 2021
The nuclear compartment is delimited by a specialized expanded sheet of the endoplasmic reticulum (ER) known as the nuclear envelope (NE). Compared to the outer nuclear membrane and the contiguous peripheral ER, the inner nuclear membrane (INM) houses a unique set of transmembrane proteins that serve a staggering range of functions.
Pawar S, Kutay U.
europepmc   +3 more sources

Making and breaking the inner nuclear membrane proteome

Current Opinion in Cell Biology, 2022
The nuclear envelope (NE) is the defining feature of eukaryotic cells, separating the nucleus from the cytoplasm. It has a complex architecture consisting of two lipid bilayers that, despite being continuous between them and with the endoplasmic reticulum, have different protein compositions consistent with their distinct functions.
Hahn, Lilli, Carvalho, Pedro
openaire   +3 more sources

Nuclear envelope proteomics: Novel integral membrane proteins of the inner nuclear membrane [PDF]

Proceedings of the National Academy of Sciences, 2001
The nuclear envelope (NE) is one of the least characterized structures of eukaryotic cells. The study of its functional roles is hampered by the small number of proteins known to be specifically located to it. Here, we present a comprehensive characterization of the NE proteome.
M, Dreger, L, Bengtsson, T, Schöneberg, H, Otto, F, Hucho   +4 more
openaire   +2 more sources

3-D Ultrastructure of O. tauri: Electron Cryotomography of an Entire Eukaryotic Cell [PDF]

, 2007
The hallmark of eukaryotic cells is their segregation of key biological functions into discrete, membrane-bound organelles. Creating accurate models of their ultrastructural complexity has been difficult in part because of the limited resolution of light
A Al-Amoudi, A Briegel, A Komeili, A Scheffel, AM van de Meene, AS Frangakis, AS Frangakis, B Farinas, B Palenik, B Storrie, C Courties, C Courties, C Suloway, CA Mannella, CA Mannella, CA Mannella, CA Mannella, CM Spahn, CV Iancu, CV Iancu, CW Akey, D Hoepfner, D Nicastro, D Stoffler, DN Mastronarde, E Derelle, E Shimoni, ER Wright, G Perkins, GC Johnston, GJ Jensen, GK Voeltz, GM Gaietta, GP Henderson, Grant J. Jensen, Gregory P. Henderson, HS Yoon, J Dubochet, J Kurner, JB Heymann, JL Hoog, JP Caviston, JP Ral, JR Warner, KL McDonald, LA Staehelin, LR Comolli, Lu Gan, M Beck, M Marko, MJ Chrétiennot-Dinet, O Medalia, PA Leong, Paul Digard, PE Purdue, Q Yang, QS Zheng, R Grimm, R Nevo, R Zadrag, RR Guillard, RT Mullen, S Robbens, S Subramaniam, SP Drummond, UC Vothknecht, V Lucic, V Stoppin, Y Shibata   +68 more
core   +13 more sources