Dynein light intermediate chains as pivotal determinants of dynein multifunctionality

ABSTRACT In animal cells, a single cytoplasmic dynein motor mediates microtubule minus-end-directed transport, counterbalancing dozens of plus-end-directed kinesins. The remarkable ability to interact with diverse cargo spectrum stems from its tightly regulated recruitment cargo-specific adaptor proteins, which engage the dynactin complex make tripartite processive motor. Adaptor binding is governed by homologous light intermediate chain subunits LIC1 (DYNC1LI1) and LIC2 (DYNC1LI2), exist in mutually exclusive complexes that can perform both unique overlapping functions. intrinsically disordered variable C-terminal domains LICs are indispensable for engaging variety structurally divergent adaptors. Here, we hypothesize numerous spatiotemporally permutations posttranslational modifications LICs, as well adaptors cargoes, exponentially expand dynein–adaptor–cargo complexes. We thematically illustrate possibilities could generate vast set biochemical variations required support wide range