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Basic Information:
| Symbol | PDZD8 | 
| Synonyms | PDZK8 | 
| Protein Name | PDZ domain-containing protein 8 (Sarcoma antigen NY-SAR-84/NY-SAR-104) | 
| Species | Human | 
| Entrez ID | 118987 | 
| Uniprot ID | Q8NEN9 | 
| Membrane Contact Site | 
                            ER-Endosome; Endosome-ER
                             
                                 | 
                    
| Location (from literature) | ER | 
| Cell line/Tissue | HEK293 cells; HeLa cells; HEK293T cells; COS-7 cells; U2-OS cells | 
| Experimental Method | Low throughput experimental methods | 
| Protein Sequence | |
| More related results | 
Complex Information:
| Complex ID | Subunit of complex | Subcellular location | Species | More | 
| CMCS00018 | PDZD8; RAB7A | ER-Endosome; Endosome-ER | Human | more | CMCS00183 | PDZD8; RAB7A; ZFYVE27 | ER-Endosome; Endosome-ER | Human | more | 
Expression Overview of PDZD8:
Homology Information of PDZD8:
| Uniprot ID | Q8NEN9 | 
| EggNOG | KOG3532 | 
| HOGENOM | CLU_008594_0_0_1 | 
| OrthoDB | 3681901at2759 | 
| TreeFam | TF324166 | 
| GeneTree | ENSGT00390000017746 | 
References:
| Pubmed ID | 31636202 | 
| DOI | 10.1073/pnas.1913509116 | 
| Description | PDZD8 mediates a Rab7-dependent interaction of the ER with late endosomes and lysosomes. | 
| Description of experimental evidence | The protein was validated by microscopy, immunofluorescence and pull-down assay in HEK293 cells and HeLa cells. | 
| More related results | 
| Pubmed ID | 33912962 | 
| DOI | 10.1242/jcs.255026 | 
| Description | PDZD8-mediated lipid transfer at contacts between the ER and late endosomes/lysosomes is required for neurite outgrowth. | 
| Description of experimental evidence | The protein was validated by confocal microscopy, live cell super-resolution Lattice-SIM microscopy, immunofluorescence staining, quantitative RT-PCR, GFP-trap assay, mass spectrometry, pulldown assays and pull-down assay in HeLa cells, HEK293T cells, COS-7 cells and U2-OS cells, which is required for LE/lys positioning and neurite outgrowth, which is dependent on the lipid transfer activity of the SMP domain. | 
| More related results |