EB1 recognizes the nucleotide state of tubulin in the microtubule lattice.

Plus-end-tracking proteins (+TIPs) are localized at the fast-growing, or plus end, of microtubules, and link microtubule ends to cellular structures. One of the best studied +TIPs is EB1, which forms comet-like structures at the tips of growing microtubules. The molecular mechanisms by which EB1 rec...

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Autores principales:	Marija Zanic, Jeffrey H Stear, Anthony A Hyman, Jonathon Howard
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2009
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/5ae4942f90084a0f96426dfb79874ee8
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spelling	oai:doaj.org-article:5ae4942f90084a0f96426dfb79874ee82021-11-25T06:28:34ZEB1 recognizes the nucleotide state of tubulin in the microtubule lattice.1932-620310.1371/journal.pone.0007585https://doaj.org/article/5ae4942f90084a0f96426dfb79874ee82009-10-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19851462/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Plus-end-tracking proteins (+TIPs) are localized at the fast-growing, or plus end, of microtubules, and link microtubule ends to cellular structures. One of the best studied +TIPs is EB1, which forms comet-like structures at the tips of growing microtubules. The molecular mechanisms by which EB1 recognizes and tracks growing microtubule ends are largely unknown. However, one clue is that EB1 can bind directly to a microtubule end in the absence of other proteins. Here we use an in vitro assay for dynamic microtubule growth with two-color total-internal-reflection-fluorescence imaging to investigate binding of mammalian EB1 to both stabilized and dynamic microtubules. We find that under conditions of microtubule growth, EB1 not only tip tracks, as previously shown, but also preferentially recognizes the GMPCPP microtubule lattice as opposed to the GDP lattice. The interaction of EB1 with the GMPCPP microtubule lattice depends on the E-hook of tubulin, as well as the amount of salt in solution. The ability to distinguish different nucleotide states of tubulin in microtubule lattice may contribute to the end-tracking mechanism of EB1.Marija ZanicJeffrey H StearAnthony A HymanJonathon HowardPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 4, Iss 10, p e7585 (2009)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Marija Zanic Jeffrey H Stear Anthony A Hyman Jonathon Howard EB1 recognizes the nucleotide state of tubulin in the microtubule lattice.
description	Plus-end-tracking proteins (+TIPs) are localized at the fast-growing, or plus end, of microtubules, and link microtubule ends to cellular structures. One of the best studied +TIPs is EB1, which forms comet-like structures at the tips of growing microtubules. The molecular mechanisms by which EB1 recognizes and tracks growing microtubule ends are largely unknown. However, one clue is that EB1 can bind directly to a microtubule end in the absence of other proteins. Here we use an in vitro assay for dynamic microtubule growth with two-color total-internal-reflection-fluorescence imaging to investigate binding of mammalian EB1 to both stabilized and dynamic microtubules. We find that under conditions of microtubule growth, EB1 not only tip tracks, as previously shown, but also preferentially recognizes the GMPCPP microtubule lattice as opposed to the GDP lattice. The interaction of EB1 with the GMPCPP microtubule lattice depends on the E-hook of tubulin, as well as the amount of salt in solution. The ability to distinguish different nucleotide states of tubulin in microtubule lattice may contribute to the end-tracking mechanism of EB1.
format	article
author	Marija Zanic Jeffrey H Stear Anthony A Hyman Jonathon Howard
author_facet	Marija Zanic Jeffrey H Stear Anthony A Hyman Jonathon Howard
author_sort	Marija Zanic
title	EB1 recognizes the nucleotide state of tubulin in the microtubule lattice.
title_short	EB1 recognizes the nucleotide state of tubulin in the microtubule lattice.
title_full	EB1 recognizes the nucleotide state of tubulin in the microtubule lattice.
title_fullStr	EB1 recognizes the nucleotide state of tubulin in the microtubule lattice.
title_full_unstemmed	EB1 recognizes the nucleotide state of tubulin in the microtubule lattice.
title_sort	eb1 recognizes the nucleotide state of tubulin in the microtubule lattice.
publisher	Public Library of Science (PLoS)
publishDate	2009
url	https://doaj.org/article/5ae4942f90084a0f96426dfb79874ee8
work_keys_str_mv	AT marijazanic eb1recognizesthenucleotidestateoftubulininthemicrotubulelattice AT jeffreyhstear eb1recognizesthenucleotidestateoftubulininthemicrotubulelattice AT anthonyahyman eb1recognizesthenucleotidestateoftubulininthemicrotubulelattice AT jonathonhoward eb1recognizesthenucleotidestateoftubulininthemicrotubulelattice
_version_	1718413682829950976

EB1 recognizes the nucleotide state of tubulin in the microtubule lattice.

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