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The unfolded protein response (UPR) is a cellular stress response related to the endoplasmic reticulum (ER) stress. [1] It has been found to be conserved between mammalian species, [2] as well as yeast [1] [3] and worm organisms. The UPR is activated in response to an accumulation of unfolded or misfolded proteins in the lumen of the
The endoplasmic reticulum (ER) is a part of a transportation system of the eukaryotic cell, and has many other important functions such as protein folding. It is a type of organelle made up of two subunits – rough endoplasmic reticulum ( RER ), and smooth endoplasmic reticulum ( SER ).
HIV uses an efficient mechanism to dislocate a single-membrane-spanning host protein, CD4, from the ER and submits it to ERAD. The Vpu protein of HIV-1 is a protein on the ER membrane and targets newly made CD4 in the endoplasmic reticulum for degradation by cytosolic proteasomes. [3] Vpu only utilizes part of the ERAD process to degrade CD4.
The fraction of ER that co-purifies with mitochondria, the so-called Mitochondria-associated endoplasmic reticulum membrane (MAM) has been extensively studied during the last decade. In the " MAM hypothesis " it has been proposed that at the centre of the pathogenesis of Alzheimer's disease resides the disorder of ER-mitochondrial contact sites ...
Ion channels are also classified according to their subcellular localization. The plasma membrane accounts for around 2% of the total membrane in the cell, whereas intracellular organelles contain 98% of the cell's membrane. The major intracellular compartments are endoplasmic reticulum, Golgi apparatus, and mitochondria. On the basis of ...
An active form of callase was found within spherosomes, but not within the endoplasmic reticulum or golgi apparatus, suggesting it is in fact the spherosomes function to degrade the cell wall. The degradation of the cell wall by the spherosomes can therefore lead to the formation of the cytomictic channels.
An electron transport chain (ETC [1]) is a series of protein complexes and other molecules which transfer electrons from electron donors to electron acceptors via redox reactions (both reduction and oxidation occurring simultaneously) and couples this electron transfer with the transfer of protons (H + ions) across a membrane.
In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation.