Melanophilin and myosin Va track the microtubule plus end on EB1
| Autor: | John A. Hammer, Xufeng S. Wu, Grace L. Tsan |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2005 |
| Předmět: |
Receptor complex
Macromolecular Substances Melanosome membrane Microtubule-associated protein Green Fluorescent Proteins Molecular Sequence Data Myosin Type V Reviews macromolecular substances Biology Microtubules rab27 GTP-Binding Proteins Cell Line Mice Microtubule Report Chlorocebus aethiops Myosin Animals Humans Amino Acid Sequence RNA Small Interfering Actin Research Articles Adaptor Proteins Signal Transducing Melanosomes fungi Comment Cell Biology Fibroblasts Actins Rats Microtubule plus-end Cell biology Gene Expression Regulation rab GTP-Binding Proteins COS Cells Melanophilin Melanocytes Carrier Proteins Microtubule-Associated Proteins HeLa Cells |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| Popis: | In mouse melanocytes, myosin Va is recruited onto the surface of melanosomes by a receptor complex containing Rab27a that is present in the melanosome membrane and melanophilin (Mlp), which links myosin Va to Rab27a. In this study, we show that Mlp is also a microtubule plus end–tracking protein or +TIP. Moreover, myosin Va tracks the plus end in a Mlp-dependent manner. Data showing that overexpression and short inhibitory RNA knockdown of the +TIP EB1 have opposite effects on Mlp–microtubule interaction, that Mlp interacts directly with EB1, and that deletion from Mlp of a region similar to one in the adenomatous polyposis coli protein involved in EB1 binding blocks Mlp's ability to plus end track argue that Mlp tracks the plus end directly by hitchhiking on EB1. These results identify a novel +TIP and indicate that vertebrate cells possess a +TIP complex that is similar to the Myo2p–Kar9p–Bim1p complex in yeast. We suggest that the +TIP complex identified in this study may serve to focus the transfer of melanosomes from microtubules to actin at the microtubule plus end. |
| Databáze: | OpenAIRE |
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