Table 3.
Proteins identified by mass spectrometry as interacting with Larp1 using lysates of two isogenic epithelial ovarian cancer cell lines, PE01 and PE04
| Cytoskeleton | Protein synthesis |
|---|---|
| (β actin | hnRNPE, G, Q2 |
| α2 (smooth muscle) actin | 40S ribosome proteins S14, S25 |
| actin prepeptide | 60S ribosome proteins L22, L23A |
| α-1, α-4 actinin | nucleolin |
| CAPZA and CAPZB | PABP |
| α-tubulin | RNA (DEAD box) helicase |
| keratins 1, 2e, 4, 5, 6B, 7, 8, 9, 10, 18, 19 | |
| LIM-domain containing protein | Transcription / chromatin |
| myosins 1, 2, 6, 9 | histones 1B, 2A, 4, testicular H1 |
| plectin 1 | Thymopoietin α (LAP2 alpha) |
| α-2 and β-spectrin | YB1 |
| Tropomysin | |
| zona occludens 1 | |
| Chaperone / cell cycle / cell signalling | |
| Metabolism | Hsp70 and 90 |
| Lactate dehydrogenase A | Protein phosphatase 1 |
| Phenylalanine hydroxylase | Ig κ light chain |
| mitotic spindle associated protein | |
| annexin A2 | |
| EF hand domain family D2 | |
| 14-3-3 σ and θ | |
| ubiquitin | |
| SUMO | |
| Clathrin | |
| SLC25A4 |
Candidate proteins identified using PABP controls were excluded. Proteins were grouped by function. This showed that Larp1 predominantly interacts with cytoskeletal proteins, but also proteins required for protein synthesis, chaperones, cell signalling, transcription and metabolism.