# Sequence and structural insights of monoleucine-based sorting motifs contained within the cytoplasmic domains of basolateral proteins

## TL;DR

This review explores a non-canonical sorting motif in proteins that target the basolateral membrane in epithelial cells.

## Contribution

The paper highlights the discovery and structural analysis of monoleucine-based sorting motifs in basolateral proteins.

## Key findings

- Six basolateral proteins were found to contain monoleucine-based sorting motifs.
- These motifs lack the canonical tyrosine- and dileucine-based sequences.
- The structural features of these motifs are conserved and require further study.

## Abstract

Delivery to the correct membrane domain in polarized epithelial cells is a critical regulatory mechanism for transmembrane proteins. The trafficking of these proteins is directed by short amino acid sequences known as sorting motifs. In six basolaterally-localized proteins lacking the canonical tyrosine- and dileucine-based basolateral sorting motifs, a monoleucine-based sorting motif has been identified. This review will discuss these proteins with an identified monoleucine-based sorting motif, their conserved structural features, as well as the future directions of study for this non-canonical basolateral sorting motif.