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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 ...
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.
COPI is a coatomer that coats the vesicles transporting proteins from the Golgi complex to the ER. [4] This pathway is referred to as retrograde transport. Before the COP I protein can coat vesicles on the Golgi membrane, it must interact with a small GTPase called ARF1 (ADP ribosylation factor). [5]
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.
The Golgi complex plays a key role in the sorting and modification of proteins exported from the endoplasmic reticulum. The protein encoded by this gene is a type II Golgi transmembrane protein. It processes protein synthesized in the rough endoplasmic reticulum and assists in the transport of protein cargo through the Golgi apparatus.
There are different AP complexes in mammals. AP1 is responsible for the transport of lysosomal hydrolases between the trans-Golgi network, and endosomes. [6] AP2 adaptor complex associates with the plasma membrane and is responsible for endocytosis. [7] AP3 is responsible for protein trafficking to lysosomes and other related organelles. [8]
Electron micrograph of in vitro–formed COPI-coated vesicles. Average vesicle diameter at the membrane level is 60 nm. COPI is a coatomer, a protein complex [1] that coats vesicles transporting proteins from the cis end of the Golgi complex back to the rough endoplasmic reticulum (ER), where they were originally synthesized, and between Golgi compartments.
The endoplasmic-reticulum–Golgi intermediate compartment (ERGIC) is an organelle in eukaryotic cells. This compartment mediates transport between the endoplasmic reticulum (ER) and Golgi complex, facilitating the sorting of cargo. [1] The cluster was first identified in 1988 using an antibody to the protein that has since been named ERGIC-53. [2]