Myosin-Vb functions as a dynamic tether for peripheral endocytic compartments during transferrin trafficking
<p>Abstract</p> <p>Background</p> <p>Myosin-Vb has been shown to be involved in the recycling of diverse proteins in multiple cell types. Studies on transferrin trafficking in HeLa cells using a dominant-negative myosin-Vb tail fragment suggested that myosin-Vb was requ...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
BMC
2008-08-01
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| Series: | BMC Cell Biology |
| Online Access: | http://www.biomedcentral.com/1471-2121/9/44 |
| _version_ | 1818755636996866048 |
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| author | Wood Patrick R Addison Erin J Provance D William Chen David Z Silan Colleen M Mercer John A |
| author_facet | Wood Patrick R Addison Erin J Provance D William Chen David Z Silan Colleen M Mercer John A |
| author_sort | Wood Patrick R |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>Myosin-Vb has been shown to be involved in the recycling of diverse proteins in multiple cell types. Studies on transferrin trafficking in HeLa cells using a dominant-negative myosin-Vb tail fragment suggested that myosin-Vb was required for recycling from perinuclear compartments to the plasma membrane. However, chemical-genetic, dominant-negative experiments, in which myosin-Vb was specifically induced to bind to actin, suggested that the initial hypothesis was incorrect both in its site and mode of myosin-Vb action. Instead, the chemical-genetic data suggested that myosin-Vb functions in the actin-rich periphery as a dynamic tether on peripheral endosomes, retarding transferrin transport to perinuclear compartments.</p> <p>Results</p> <p>In this study, we employed both approaches, with the addition of overexpression of full-length wild-type myosin-Vb and switching the order of myosin-Vb inhibition and transferrin loading, to distinguish between these hypotheses. Overexpression of full-length myosin-Vb produced large peripheral endosomes. Chemical-genetic inhibition of myosin-Vb after loading with transferrin did not prevent movement of transferrin from perinuclear compartments; however, virtually all myosin-Vb-decorated particles, including those moving on microtubules, were halted by the inhibition. Overexpression of the myosin-Vb tail caused a less-peripheral distribution of early endosome antigen-1 (EEA1).</p> <p>Conclusion</p> <p>All results favored the peripheral dynamic tethering hypothesis.</p> |
| first_indexed | 2024-12-18T05:42:18Z |
| format | Article |
| id | doaj.art-8e4a408a22ea41f793087c5520f77738 |
| institution | Directory Open Access Journal |
| issn | 1471-2121 |
| language | English |
| last_indexed | 2024-12-18T05:42:18Z |
| publishDate | 2008-08-01 |
| publisher | BMC |
| record_format | Article |
| series | BMC Cell Biology |
| spelling | doaj.art-8e4a408a22ea41f793087c5520f777382022-12-21T21:19:08ZengBMCBMC Cell Biology1471-21212008-08-01914410.1186/1471-2121-9-44Myosin-Vb functions as a dynamic tether for peripheral endocytic compartments during transferrin traffickingWood Patrick RAddison Erin JProvance D WilliamChen David ZSilan Colleen MMercer John A<p>Abstract</p> <p>Background</p> <p>Myosin-Vb has been shown to be involved in the recycling of diverse proteins in multiple cell types. Studies on transferrin trafficking in HeLa cells using a dominant-negative myosin-Vb tail fragment suggested that myosin-Vb was required for recycling from perinuclear compartments to the plasma membrane. However, chemical-genetic, dominant-negative experiments, in which myosin-Vb was specifically induced to bind to actin, suggested that the initial hypothesis was incorrect both in its site and mode of myosin-Vb action. Instead, the chemical-genetic data suggested that myosin-Vb functions in the actin-rich periphery as a dynamic tether on peripheral endosomes, retarding transferrin transport to perinuclear compartments.</p> <p>Results</p> <p>In this study, we employed both approaches, with the addition of overexpression of full-length wild-type myosin-Vb and switching the order of myosin-Vb inhibition and transferrin loading, to distinguish between these hypotheses. Overexpression of full-length myosin-Vb produced large peripheral endosomes. Chemical-genetic inhibition of myosin-Vb after loading with transferrin did not prevent movement of transferrin from perinuclear compartments; however, virtually all myosin-Vb-decorated particles, including those moving on microtubules, were halted by the inhibition. Overexpression of the myosin-Vb tail caused a less-peripheral distribution of early endosome antigen-1 (EEA1).</p> <p>Conclusion</p> <p>All results favored the peripheral dynamic tethering hypothesis.</p>http://www.biomedcentral.com/1471-2121/9/44 |
| spellingShingle | Wood Patrick R Addison Erin J Provance D William Chen David Z Silan Colleen M Mercer John A Myosin-Vb functions as a dynamic tether for peripheral endocytic compartments during transferrin trafficking BMC Cell Biology |
| title | Myosin-Vb functions as a dynamic tether for peripheral endocytic compartments during transferrin trafficking |
| title_full | Myosin-Vb functions as a dynamic tether for peripheral endocytic compartments during transferrin trafficking |
| title_fullStr | Myosin-Vb functions as a dynamic tether for peripheral endocytic compartments during transferrin trafficking |
| title_full_unstemmed | Myosin-Vb functions as a dynamic tether for peripheral endocytic compartments during transferrin trafficking |
| title_short | Myosin-Vb functions as a dynamic tether for peripheral endocytic compartments during transferrin trafficking |
| title_sort | myosin vb functions as a dynamic tether for peripheral endocytic compartments during transferrin trafficking |
| url | http://www.biomedcentral.com/1471-2121/9/44 |
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