AGFG1 (HRB) is a nucleocytoplasmic adaptor protein that links the clathrin-dependent endocytic machinery to nucleocytoplasmic transport [PMID:18819912, PMID:10613896]. In the cytoplasm it colocalizes with clathrin-, AP-2-, EPS15-, and transferrin receptor-containing vesicles and binds the vesicular SNARE TI-VAMP (VAMP7); its depletion strongly reduces endocytosis of transferrin and TI-VAMP, establishing it as a required component of clathrin-dependent endocytosis PMID:18819912. AGFG1 also associates with the EH-domain proteins Eps15 and Eps15R through its EH-binding motifs, an interaction that occurs in the cytoplasm and that synergizes with AGFG1 to enhance Rev-mediated nuclear export PMID:10613896. Beyond these endocytic and Rev-export roles, no further mechanistic detail has been characterized in the available corpus.
Recorded for reference. The AIGR evaluation found this grounding is coarse (collapses to general parents) and can contradict the narrative — do not import these GO ids directly; re-ground from the narrative + PMIDs.
| Year | Confidence | Finding | PMIDs | Journal |
|---|---|---|---|---|
| 2008 | High | HRB (AGFG1) was identified as a binding partner of the vesicular SNARE TI-VAMP (VAMP7) by yeast two-hybrid screening and confirmed by biochemical assays. In HeLa cells, HRB localized to the nucleus and cytoplasm, with cytoplasmic HRB colocalizing with clathrin-, AP-2-, EPS15-, and transferrin receptor-containing vesicles. Knockdown of HRB strongly reduced endocytosis of fluorescent transferrin and pHLuorin-TI-VAMP as measured by FACS, establishing HRB as a required component of clathrin-dependent endocytosis. | PMID:18819912 | The Journal of biological chemistry |
| 1999 | Medium | HRB (AGFG1) interacts with the EH (Eps15 homology) domain-containing proteins Eps15 and Eps15R via its EH-binding motifs, and this interaction occurs in the cytoplasm. Eps15 and Eps15R synergize with HRB to enhance Rev-mediated nuclear export function, and the EH-mediated Eps15–HRB interaction is required for this synergistic effect, connecting the endocytic molecular machinery to nucleocytoplasmic transport. | PMID:10613896 | The Journal of cell biology |