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Jump-starting kinesin
When it is not actively transporting cargo, conventional Kinesin-1 is present in the cytoplasm in a folded conformation that cannot interact effectively with microtubules (MTs). Two important and largely unexplored aspects of kinesin regulation are how it is converted to an active species when bound...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
2007
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2063616/ https://www.ncbi.nlm.nih.gov/pubmed/17200413 http://dx.doi.org/10.1083/jcb.200611082 |
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author | Hackney, David D. |
author_facet | Hackney, David D. |
author_sort | Hackney, David D. |
collection | PubMed |
description | When it is not actively transporting cargo, conventional Kinesin-1 is present in the cytoplasm in a folded conformation that cannot interact effectively with microtubules (MTs). Two important and largely unexplored aspects of kinesin regulation are how it is converted to an active species when bound to cargo and the related issue of how kinesin discriminates among its many potential cargo molecules. Blasius et al. (see p. 11 of this issue) report that either binding of the cargo linker c-Jun N-terminal kinase–interacting protein 1 (JIP1) to the light chains (LCs) or binding of fasciculation and elongation protein ζ1 (FEZ1) to the heavy chains (HCs) is insufficient for activation but that activation occurs when both are present simultaneously. A related paper by Cai et al. (see p. 51 of this issue) provides structural insight into the conformation of the folded state in the cell obtained by fluorescence resonance energy transfer analysis. |
format | Text |
id | pubmed-2063616 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2007 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-20636162007-11-29 Jump-starting kinesin Hackney, David D. J Cell Biol Reviews When it is not actively transporting cargo, conventional Kinesin-1 is present in the cytoplasm in a folded conformation that cannot interact effectively with microtubules (MTs). Two important and largely unexplored aspects of kinesin regulation are how it is converted to an active species when bound to cargo and the related issue of how kinesin discriminates among its many potential cargo molecules. Blasius et al. (see p. 11 of this issue) report that either binding of the cargo linker c-Jun N-terminal kinase–interacting protein 1 (JIP1) to the light chains (LCs) or binding of fasciculation and elongation protein ζ1 (FEZ1) to the heavy chains (HCs) is insufficient for activation but that activation occurs when both are present simultaneously. A related paper by Cai et al. (see p. 51 of this issue) provides structural insight into the conformation of the folded state in the cell obtained by fluorescence resonance energy transfer analysis. The Rockefeller University Press 2007-01-01 /pmc/articles/PMC2063616/ /pubmed/17200413 http://dx.doi.org/10.1083/jcb.200611082 Text en Copyright © 2007, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Reviews Hackney, David D. Jump-starting kinesin |
title | Jump-starting kinesin |
title_full | Jump-starting kinesin |
title_fullStr | Jump-starting kinesin |
title_full_unstemmed | Jump-starting kinesin |
title_short | Jump-starting kinesin |
title_sort | jump-starting kinesin |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2063616/ https://www.ncbi.nlm.nih.gov/pubmed/17200413 http://dx.doi.org/10.1083/jcb.200611082 |
work_keys_str_mv | AT hackneydavidd jumpstartingkinesin |