GOLPH1, also known as GCP60, was initially identified as a Golgi protein that can interact with the integral membrane protein giantin and is thought to be involved in the maintenance of the Golgi structure. GOLPH1 has also been shown to interact with other Golgi proteins such as Golgin-160, a Golgi protein that can be cleaved by caspases-2, -3, and -7, leading to the nuclear localization of Golgin-160. GOLPH1 interaction with the Golgin-160 fragments is stronger than that with the intact Golgin-160, with its interaction regulated by the oxidation state of Cys-463 within GOLPH1, suggesting that the nuclear localization of the caspase-cleaved Golgin-160 fragments is a highly coordinated event. GOLPH1 has also been found to interact with Numb, a cytosolic signaling protein that mediates asymetric cell division of neural progenitor cells to a daughter progenitor cell and a neuron, suggesting that Golgi fragmentation and reconstitution during the cell cycle differentially regulate Numb signaling through changes in GOLPH1 subcellular distribution and may couple cell fate with cell cycle progression.
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Protein Aliases: Acyl-CoA-binding domain-containing protein 3; acyl-Coenzyme A binding domain containing 3; DAP; DMT1-associated protein; GOCAP1; golgi complex associated protein 1, 60 kDa; golgi complex associated protein 1, 60kDa; Golgi complex-associated protein 1; Golgi phosphoprotein 1; Golgi resident protein GCP60; Golgi resident protein GCP60, N-terminally processed; GOLPH1; neurotrophin receptor alike death domain protein; p75-like apoptosis-inducing death domain protein; PBR associated protein; PBR- and PKA-associated protein 7; Peripheral benzodiazepine receptor-associated protein PAP7; peripherial benzodiazepine receptor associated protein; PKA (RIalpha)-associated protein
Gene Aliases: 60kDa; 8430407O11Rik; ACBD3; D1Ertd10e; GCP60; GOCAP1; GOLPH1; PAP7