6ku0
Crystal structure of MyoVa-GTD in complex with MICAL1-GTBMCrystal structure of MyoVa-GTD in complex with MICAL1-GTBM
Structural highlights
FunctionMYO5A_MOUSE Processive actin-based motor that can move in large steps approximating the 36-nm pseudo-repeat of the actin filament. Involved in melanosome transport. Also mediates the transport of vesicles to the plasma membrane. May also be required for some polarization process involved in dendrite formation.[1] Publication Abstract from PubMedMotor-mediated intracellular trafficking requires motors to position cargoes at proper locations. Myosin Va (MyoVa), an actin-based motor, is a classic model for studying cargo transport. However, the molecular basis underlying cargo unloading in MyoVa-mediated transport has remained enigmatic. We have identified MICAL1, an F-actin disassembly regulator, as a binding partner of MyoVa and shown that MICAL1-MyoVa interaction is critical for localization of MyoVa at the midbody. By binding to MICAL1, MyoVa-mediated transport is terminated, resulting in vesicle unloading at the midbody for efficient cytokinesis. The MyoVa/MICAL1 complex structure reveals that MICAL1 and F-actin assembly factors, Spires, share an overlapped binding surface on MyoVa, suggesting a regulatory role of F-actin dynamics in cargo unloading. Down-regulating F-actin disassembly by a MICAL1 mutant significantly reduces MyoVa and vesicles accumulating at the midbody. Collectively, our findings demonstrate that MyoVa binds to MICAL1 at the midbody destination and triggers F-actin disassembly to unload the vesicle cargo. F-actin disassembly factor MICAL1 binding to Myosin Va mediates cargo unloading during cytokinesis.,Niu F, Sun K, Wei W, Yu C, Wei Z Sci Adv. 2020 Nov 6;6(45). pii: 6/45/eabb1307. doi: 10.1126/sciadv.abb1307. Print, 2020 Nov. PMID:33158857[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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