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- W3163238175 abstract "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 of dynein to interact with a diverse cargo spectrum stems from its tightly regulated recruitment of cargo-specific adaptor proteins, which engage the dynactin complex to make a tripartite processive motor. Adaptor binding is governed by the homologous dynein light intermediate chain subunits LIC1 (DYNC1LI1) and LIC2 (DYNC1LI2), which exist in mutually exclusive dynein complexes that can perform both unique and overlapping functions. The intrinsically disordered and variable C-terminal domains of the LICs are indispensable for engaging a variety of structurally divergent adaptors. Here, we hypothesize that numerous spatiotemporally regulated permutations of posttranslational modifications of the LICs, as well as of the adaptors and cargoes, exponentially expand the spectrum of dynein–adaptor–cargo complexes. We thematically illustrate the possibilities that could generate a vast set of biochemical variations required to support the wide range of dynein functions." @default.
- W3163238175 created "2021-05-24" @default.
- W3163238175 creator A5050163554 @default.
- W3163238175 creator A5054676592 @default.
- W3163238175 creator A5082030444 @default.
- W3163238175 creator A5082924491 @default.
- W3163238175 date "2021-05-15" @default.
- W3163238175 modified "2023-10-06" @default.
- W3163238175 title "Dynein light intermediate chains as pivotal determinants of dynein multifunctionality" @default.
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