Rab36 regulates the spatial distribution of late endosomes and lysosomes through a similar mechanism to Rab34

Abstract

Small GTPase Rab36 is homologous to Rab34 with 56% amino acid sequence identity. Rab34 was characterized as a Golgi-associated Rab protein and regulates lysosomal positioning through interaction with RILP; however, the properties and functions of Rab36 have not been investigated. To investigate Rab36, we constructed EGFP-Rab36 wild type, the active GTP-bound mutant EGFP-Rab36Q116L and negative GDP-bound mutant EGFP-Rab36T71N. Expression of EGFP-Rab36 wild type revealed that Rab36 co-localized with Golgi markers GM130, Syntaxin 5 and TGN46 in Hela cells, indicating Rab36 is associated with Golgi apparatus. Over-expression of Rab36 induced late endosome and lysosome clustering around the Golgi apparatus, marked by LBPA, CD63, Lamp1 and Lamp2, without effects on early endosomal compartment marked by EEA1. GST-pulldown assay demonstrated that Rab36 can also interact with RILP. In addition, the binding region for Rab36 is in the C-terminal region (aa199-401) of RILP. Our data suggested that Rab36 may regulate the spatial distribution of late endosomes and lysosomes through a similar mechanism to Rab34.

Keywords::

• Rab36
• Rab34
• RILP
• late endosome
• lysosome

Acknowledgements

This work was supported by the start-up fund for new investigators from Xiamen University, China, grant No. 1280X12104.

Declaration of interest: The authors report no conflicts of interest. The authors alone are responsible for the content and writing of the paper.