# The Interaction of pT73-Rab10 with Myosin Va, but Not Myosin Vb, Is Regulated Though a Site in the Globular Tail Domain

## TL;DR

This paper shows that a specific phosphorylated form of Rab10 interacts with Myosin Va but not Myosin Vb due to a unique amino acid sequence in the Myosin Va tail.

## Contribution

The study identifies a three-amino-acid sequence in MYO5A's tail that is essential for pT73-Rab10 binding and absent in MYO5B.

## Key findings

- pT73-Rab10 does not associate with the globular tail of MYO5B.
- A three-amino-acid sequence (MEN) in MYO5A's tail is required for pT73-Rab10 binding.
- Substituting the MEN sequence in MYO5B allows it to bind pT73-Rab10.

## Abstract

The phosphorylation of Rab10 (pT73-Rab10) by LRRK2 promotes the establishment of epithelial cell polarity by controlling the trafficking to the primary cilia membrane of cilia-resident proteins and signaling proteins. Previous studies have identified a site in the globular tail domain of MYO5A that specifically binds to only the phosphorylated form of Rab10. In this work, we have demonstrated that pT73-Rab10 does not associate with the globular tail of MYO5B. We have mapped the putative binding site to a required three amino acids (MEN, 1473–1475) in the MYO5A globular tail domain that are not found in the MYO5B globular tail. Substitution of the MEN amino acid sequence found in MYO5A into the paralogous position in the MYO5B globular tail conferred the ability to associate with pT73-Rab10. The results demonstrate that the interactors with MYO5A and MYO5B are not completely overlapping and that the interaction of pT73-Rab10 is specific to the MYO5A globular tail domain.