Rab33 proteins (Rab33A and Rab33B) are small GTPases regulating vesicular transport. Key characteristics include:
Rab33B binds Atg16L1 to regulate autophagosome formation. Mutations (e.g., Atg16L1 T168A) abolish this interaction, impairing autophagy initiation .
Co-immunoprecipitation studies confirm Rab33B preferentially interacts with GTP-bound Atg16L1 .
Focal Adhesion Dynamics: Rab33B depletion via siRNA increases cell migration velocity by 20% and reduces focal adhesion (FA) size by 20%, while accelerating FA disassembly by 40% .
Exocyst Interaction: Rab33B recruits Exoc6 to secretory vesicles, mediating β1-integrin delivery to FAs. Rab33B knockdown reduces Exoc6-positive vesicles at leading edges by 25% .
Cancer Relevance: Rab33B expression inversely correlates with lung cancer progression and metastasis (TCGA data) .
Localization Studies: Immunofluorescence confirms Rab33B’s Golgi and secretory vesicle localization .
Functional Assays: Antibodies enable validation of Rab33B’s role in FA dynamics through siRNA rescue experiments (e.g., GFP-Rab33B restores migration rates) .
Protein Interaction Analysis: Co-immunoprecipitation identifies Rab33B’s binding partners (Atg16L1, Exoc6) and GTPase activity dependence .
| Parameter | Effect of Rab33B Depletion | Source |
|---|---|---|
| Cell Migration Velocity | ↑ 20% | |
| FA Assembly Rate | ↓ 20% | |
| FA Disassembly Rate | ↑ 40% | |
| Exoc6 Vesicles at Leading Edge | ↓ 25% | |
| β1-Integrin Delivery to FAs | Impaired |
KEGG: cel:CELE_F43D9.2
STRING: 6239.F43D9.2