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Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate destinations within or outside the cell. [ 1 ] [ 2 ] [ note 1 ] Proteins can be targeted to the inner space of an organelle , different intracellular membranes , the plasma membrane , or to the exterior of the cell via secretion .
VPS35 binds with other proteins to form the retromer, an evolutionarily conserved complex that plays a major role in transmembrane protein recycling from endosomes to the trans-Golgi network . [1] [6] [7] [8] VPS35 itself folds into a secondary structure that represents an α-helical solenoid, containing 34 α-helix repeats. [16]
The Golgi apparatus (/ ˈ ɡ ɒ l dʒ i /), also known as the Golgi complex, Golgi body, or simply the Golgi, is an organelle found in most eukaryotic cells. [1] Part of the endomembrane system in the cytoplasm , it packages proteins into membrane-bound vesicles inside the cell before the vesicles are sent to their destination.
As well as the location of the cis and trans Golgi network. The cis Golgi network is the first step in the cisternal structure of a protein being packaged, while the trans Golgi network is the last step in the cisternal structure when the vesicle is being transferred to either the lysosome, the cell surface or the secretory vesicle.
As a sorting receptor on the cell surface and on the endoplasmic reticulum-Golgi apparatus within the cell, sortilin is involved in the transport of a wide variety of intracellular proteins between the trans-Golgi network, endosome, lysosome, and secretory granules, as well as the plasma membrane. [8]
The protein encoded by this gene may control steps in the cycling of proteins through the trans-Golgi network to endosomes, lysosomes and the plasma membrane. Mutations in this gene cause the autosomal recessive disorder, chorea acanthocytosis. Alternative splicing of this gene results in multiple transcript variants. [7]
The encoded protein is a component of a large multimeric complex, termed the retromer complex, involved in retrograde transport of proteins from endosomes to the trans-Golgi network. The close structural similarity between the yeast and human proteins that make up this complex suggests a similarity in function.
Retromer is a complex of proteins that has been shown to be important in recycling transmembrane receptors from endosomes to the trans-Golgi network (TGN) and directly back to the plasma membrane. Mutations in retromer and its associated proteins have been linked to Alzheimer's and Parkinson's diseases. [1] [2] [3] [4]