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Rab11FIP proteins link endocytic recycling vesicles for cytoskeletal transport and tethering

Regulated trafficking of internalised integrins and growth factor receptors enables polarisation of morphology and motility and enables lumen formation in multicellular structures. Recycling vesicles marked with Rab11 direct internalised cargo back to the plasma membrane to affect biological process...

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Autor principal: Machesky, Laura M.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6356010/
https://www.ncbi.nlm.nih.gov/pubmed/30622149
http://dx.doi.org/10.1042/BSR20182219
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author Machesky, Laura M.
author_facet Machesky, Laura M.
author_sort Machesky, Laura M.
collection PubMed
description Regulated trafficking of internalised integrins and growth factor receptors enables polarisation of morphology and motility and enables lumen formation in multicellular structures. Recycling vesicles marked with Rab11 direct internalised cargo back to the plasma membrane to affect biological processes such as polarised trafficking and cancer cell invasion. A recent study by Ji and colleagues, provides insight into how the trafficking protein Rab11FIP2 links with the actin-based motor myo5b and the small GTPase Rab11 to regulate vesicle tethering and transport along actin filaments [1]. The authors used biochemical methods to demonstrate that Rab11a binds directly to the tail of myo5b and that Rab11FIP2 also forms direct interactions with both Rab11a and myo5b tails. These proteins essentially compete for binding to similar regions and thus can regulate the association and activity of each other. Ji and colleagues further demonstrate that Rab11a activates myo5b by binding to its globular tail and relieving a head-tail autoinhibition. Due to differing affinities between Rab11 and myo5b or Rab11FIP2, they propose that Rab11FIP2 mediates the association of myo5b with cargo vesicles, while Rab11a regulates the motor activity of myo5b. The present study thus elucidates how myo5b is regulated by its interactions with Rab11a and Rab11FIP2 and proposes a model for coordination of recycling vesicle tethering and motor activity. The present study has implications for how cells control polarity and motility in health and disease and suggests how Rab11FIP proteins might control motor protein activity and engagement for transport.
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spelling pubmed-63560102019-02-05 Rab11FIP proteins link endocytic recycling vesicles for cytoskeletal transport and tethering Machesky, Laura M. Biosci Rep Commentaries Regulated trafficking of internalised integrins and growth factor receptors enables polarisation of morphology and motility and enables lumen formation in multicellular structures. Recycling vesicles marked with Rab11 direct internalised cargo back to the plasma membrane to affect biological processes such as polarised trafficking and cancer cell invasion. A recent study by Ji and colleagues, provides insight into how the trafficking protein Rab11FIP2 links with the actin-based motor myo5b and the small GTPase Rab11 to regulate vesicle tethering and transport along actin filaments [1]. The authors used biochemical methods to demonstrate that Rab11a binds directly to the tail of myo5b and that Rab11FIP2 also forms direct interactions with both Rab11a and myo5b tails. These proteins essentially compete for binding to similar regions and thus can regulate the association and activity of each other. Ji and colleagues further demonstrate that Rab11a activates myo5b by binding to its globular tail and relieving a head-tail autoinhibition. Due to differing affinities between Rab11 and myo5b or Rab11FIP2, they propose that Rab11FIP2 mediates the association of myo5b with cargo vesicles, while Rab11a regulates the motor activity of myo5b. The present study thus elucidates how myo5b is regulated by its interactions with Rab11a and Rab11FIP2 and proposes a model for coordination of recycling vesicle tethering and motor activity. The present study has implications for how cells control polarity and motility in health and disease and suggests how Rab11FIP proteins might control motor protein activity and engagement for transport. Portland Press Ltd. 2019-01-30 /pmc/articles/PMC6356010/ /pubmed/30622149 http://dx.doi.org/10.1042/BSR20182219 Text en © 2019 The Author(s). http://creativecommons.org/licenses/by/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY) (http://creativecommons.org/licenses/by/4.0/) .
spellingShingle Commentaries
Machesky, Laura M.
Rab11FIP proteins link endocytic recycling vesicles for cytoskeletal transport and tethering
title Rab11FIP proteins link endocytic recycling vesicles for cytoskeletal transport and tethering
title_full Rab11FIP proteins link endocytic recycling vesicles for cytoskeletal transport and tethering
title_fullStr Rab11FIP proteins link endocytic recycling vesicles for cytoskeletal transport and tethering
title_full_unstemmed Rab11FIP proteins link endocytic recycling vesicles for cytoskeletal transport and tethering
title_short Rab11FIP proteins link endocytic recycling vesicles for cytoskeletal transport and tethering
title_sort rab11fip proteins link endocytic recycling vesicles for cytoskeletal transport and tethering
topic Commentaries
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6356010/
https://www.ncbi.nlm.nih.gov/pubmed/30622149
http://dx.doi.org/10.1042/BSR20182219
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