Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1.

摘要: The interaction of cytoplasmic dynein with its cargoes is thought to be indirectly mediated by dynactin, a complex that binds the intermediate chain. However, roles other subunits in cargo binding have been unknown. Here we demonstrate translocates rhodopsin-bearing vesicles along microtubules. This occurs directly between C-terminal tail rhodopsin and Tctex-1, light mutations responsible for retinitis pigmentosa inhibit this interaction. Our results point an alternative docking mechanism dynein, provide novel insights into role motor proteins polarized transport post-Golgi vesicles, shed on molecular basis pigmentosa.