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| Field | Value |
|---|---|
| Namespace | Cellular component |
| Short description | AP-type membrane coat adaptor complex |
| Full defintion | Any of several heterotetrameric complexes that link clathrin (or another coat-forming molecule, as hypothesized for AP-3 and AP-4) to a membrane surface; they are found on coated pits and coated vesicles, and mediate sorting of cargo proteins into vesicles. Each AP complex contains two large (a beta and one of either an alpha, gamma, delta, or epsilon) subunits (110-130 kDa), a medium (mu) subunit (approximately 50 kDa), and a small (sigma) subunit (15-20 kDa). |
| Subterm of |
The relationship of GO:0030119 with other GO terms.
| Relationship type | GO terms |
|---|---|
| Is a | |
| Regulates | n.a. |
| Part of | |
| Positively regulates | n.a. |
| Negatively regulates | n.a. |
A force layout showing the ancestor tree for GO:0030119, and its immediate children. If you wish to explore the tree dynamically, please use the GO Explorer.
This table contains additional metadata associated with the GO entry's definition field.
| Field | Value |
|---|---|
| GOC | mah |
| PMID | Adaptors for clathrin coats: structure and function. Annu Rev Cell Dev Biol. 2004; 20 (): 153–91.PMID: 15473838 Clathrin-coated vesicles (CCVs) are responsible for the transport of proteins between various compartments of the secretory and endocytic systems. Clathrin forms a scaffold around these vesicles that is linked to membranes by clathrin adaptors. The adaptors simultaneously bind to clathrin and to transmembrane proteins and/or phospholipids and can also interact with each other and with other components of the CCV formation machinery. The result is a collection of proteins that can make multiple, moderate strength (microM Kd) interactions and thereby establish the dynamic regulatable networks to drive vesicle genesis at the correct time and place in the cell. This review focuses on the structure of clathrin adaptors and how these structures provide functional information on the mechanism of CCV formation. |
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .