Search results
Results from the WOW.Com Content Network
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]
n/a Ensembl ENSG00000152291 n/a UniProt O43493 n/a RefSeq (mRNA) NM_006464 NM_001206840 NM_001206841 NM_001206844 NM_001368095 NM_001368096 n/a RefSeq (protein) NP_001193769 NP_001193770 NP_001193773 NP_006455 NP_001355024 NP_001355025 n/a Location (UCSC) Chr 2: 85.32 – 85.33 Mb n/a PubMed search n/a Wikidata View/Edit Human Trans-Golgi network integral membrane protein 2 is a protein that ...
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.
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 golgins are a family of proteins, of which the protein encoded by this gene is a member, that are localized to the Golgi. This protein has been postulated to play a role in Rab6-regulated membrane-tethering events in the Golgi apparatus. Alternative splice variants have been described but their full-length nature has not been determined. [6]
The Golgi matrix is a collection of proteins involved in the structure and function of the Golgi apparatus. [1] [2] [3] The matrix was first isolated in 1994 as an amorphous collection of 12 proteins that remained associated together in the presence of detergent (which removed Golgi membranes) and 150 m M NaCl (which removed weakly associated proteins). [4]
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.