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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. The word endoplasmic means "within the cytoplasm", and reticulum is Latin for "little net".
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 implications for the division in the four types are especially manifest at the time of translocation and ER-bound translation, when the protein has to be passed through the ER membrane in a direction dependent on the type. [citation needed] Group I and II transmembrane proteins have opposite final topologies.
The suffix -ome as used in molecular biology refers to a totality of some sort; it is an example of a "neo-suffix" formed by abstraction from various Greek terms in -ωμα, a sequence that does not form an identifiable suffix in Greek. Functional genomics aims at identifying the functions of as many genes as possible of a given organism. It ...
The endoplasmic reticulum membrane protein complex (EMC) is a putative endoplasmic reticulum-resident membrane protein (co-)chaperone. [1] The EMC is evolutionarily conserved in eukaryotes (animals, plants, and fungi), and its initial appearance might reach back to the last eukaryotic common ancestor (LECA). [ 2 ]
The N-linked glycosylation process occurs in eukaryotes in the lumen of the endoplasmic reticulum and widely in archaea, but very rarely in bacteria. In addition to their function in protein folding and cellular attachment, the N-linked glycans of a protein can modulate a protein's function, in some cases acting as an on/off switch.