Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain.

摘要: HEF1, p130(Cas), and Efs define a family of multidomain docking proteins which plays central coordinating role for tyrosine-kinase-based signaling related to cell adhesion. HEF1 function has been specifically implicated in pathways important adhesion differentiation lymphoid epithelial cells. While the SH3 domains SH2-binding site (substrate domains) are well characterized binding partners known, date highly conserved carboxy-terminal three have lacked functional definition. In this study, we determined that domain contains divergent helix-loop-helix (HLH) motif. This motif mediates homodimerization heterodimerization with recognition specificity similar transcriptional regulatory HLH Id2, E12, E47. We had previously demonstrated carboxy-terminus expressed as separate yeast reprograms division patterns, inducing constitutive pseudohyphal growth. Here show induction by requires an intact HLH, further supporting idea effector activity implying derives part from interactions proteins. These combined results provide initial insight into mode suggest protein may interact cellular control differentiation.