Interactions in protein complexes can be predicted from evolutionary information from genomic sequences.

Hox genes are activated sequentially and, at the same time, undergo a transition from an inactive to an active chromatin compartment, most likely to prevent posterior genes being activated too early.

The Hox transcription factor Ultrabithorax (Ubx) represses alternative gene programs during lineage development by lineage-specific Polycomb protein complex retention at Ubx-targeted chromatin sites.

Interactions between Hox and TALE genes, which generate bilaterally symmetrical body plans, originated in early multicellular animals.

Nup98-HoxA9 is recruited to Hox gene cluster regions together with the chromosomally pre-bound nuclear export factor Crm1, which induces aberrant expression of several Hox genes and affecting the differentiation of embryonic stem cells.

The collinear activation of a subset of posterior Hox genes is responsible for establishing a Wnt/T activity gradient that is required to generate the complete body axis, and hence the full set of segments within a vertebrate embryo.

Tuned protein–protein interaction affinity optimizes the repressive function of the ETS family transcription factor Yan in order to contribute specificity and robustness to cell fate specification in the developing Drosophila eye.

The tethering complex HOPS employs affinity for each of the 4 SNAREs to catalyze assembly of 3-SNARE intermediates, supporting an immediate burst of membrane fusion triggered by the 4th SNARE.

Genetic analyses reveal that the loss of Lin28a causes axial shortening with mild skeletal transformations via decreased PRC1 at Hox genes, establishing a new pathway in the “Hox code.”.

Short peptide motifs can confer specificity to developmental networks by inhibiting protein–protein interactions.