Fig. 6.

Model of L1 conformational regulation by cytoplasmic modifications. L1 has been shown to exist in distinct conformations on the cell surface [19]. These conformations have been shown to involve T1172 phosphorylation [19], and T1172 phosphorylation has been shown to be regulated by the conformation of the L1 cytoplasmic tail [29]. We propose a model whereby T1172 availability is regulated at least in part by unfolding of the L1 cytoplasmic domain that is triggered by deamidation of N1251. The ramifications of this event (e.g., proteolysis and signaling) are shown. Y tyrosine, N asparagine, D aspartate, isoD iso-aspartate