Fattening the perspective of Hox protein specificity through SLiMming.

The functional identification and dissection of protein domains has been a successful approach towards the understanding of Hox protein specificity. However, only a few functional protein domains have been identified; this has been a major limitation in deciphering the molecular modalities of Hox protein action. We explore here, by in silico survey of short linear motifs (SLiMs) in Hox proteins, the contribution of SLiMs to Hox proteins, focusing on the mouse, chick and Drosophila Hox complement. Our findings reveal a widespread and uniform distribution of SLiMs along Hox protein sequences and identify the most apparent features of Hox associated SLiMs. While few motifs have been associated with Hox proteins so far, this work suggests that many more contribute to Hox protein functions. The potential and difficulties to apprehend the full contribution of SLiMs in controlling Hox protein functions are discussed.