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The endoplasmic reticulum is found in most eukaryotic cells and forms an interconnected network of flattened, membrane-enclosed sacs known as cisternae (in the RER), and tubular structures in the SER. The membranes of the ER are continuous with the outer nuclear membrane. The endoplasmic reticulum is not found in red blood cells, or spermatozoa.
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
ER retention refers to proteins that are retained in the endoplasmic reticulum, or ER, after folding; these are known as ER resident proteins. Protein localization to the ER often depends on certain sequences of amino acids located at the N terminus or C terminus. These sequences are known as signal peptides, molecular signatures, or sorting ...
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 ...
As the labor market cools, data suggests more workers are getting "dry promoted" and taking on more responsibilities or a new title for the same pay.
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.