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MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties

We observe that one of the high molecular mass microtubule-associated proteins (MAPs) from brain exhibits nucleotide-dependent binding to microtubules. We identify the protein as MAP IC, which was previously described in this laboratory as a minor component of standard microtubule preparations (Bloo...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1987
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Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114794/
https://www.ncbi.nlm.nih.gov/pubmed/2958482
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collection PubMed
description We observe that one of the high molecular mass microtubule-associated proteins (MAPs) from brain exhibits nucleotide-dependent binding to microtubules. We identify the protein as MAP IC, which was previously described in this laboratory as a minor component of standard microtubule preparations (Bloom, G.S., T. Schoenfeld, and R.B. Vallee, 1984, J. Cell Biol., 98:320-330). We find that MAP 1C is enriched in microtubules prepared in the absence of nucleotide. Kinesin is also found in these preparations, but can be specifically extracted with GTP. A fraction highly enriched in MAP 1C can be prepared by subsequent extraction of the microtubules with ATP. Two activities cofractionate with MAP 1C upon further purification, a microtubule-activated ATPase activity and a microtubule-translocating activity. These activities indicate a role for the protein in cytoplasmic motility. MAP 1C coelectrophoreses with the beta heavy chain of Chlamydomonas flagellar dynein, and has a sedimentation coefficient of 20S. Exposure to ultraviolet light in the presence of vanadate and ATP results in the production of two large fragments of MAP 1C. These characteristics suggest that MAP 1C may be a cytoplasmic analogue of axonemal dynein.
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spelling pubmed-21147942008-05-01 MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties J Cell Biol Articles We observe that one of the high molecular mass microtubule-associated proteins (MAPs) from brain exhibits nucleotide-dependent binding to microtubules. We identify the protein as MAP IC, which was previously described in this laboratory as a minor component of standard microtubule preparations (Bloom, G.S., T. Schoenfeld, and R.B. Vallee, 1984, J. Cell Biol., 98:320-330). We find that MAP 1C is enriched in microtubules prepared in the absence of nucleotide. Kinesin is also found in these preparations, but can be specifically extracted with GTP. A fraction highly enriched in MAP 1C can be prepared by subsequent extraction of the microtubules with ATP. Two activities cofractionate with MAP 1C upon further purification, a microtubule-activated ATPase activity and a microtubule-translocating activity. These activities indicate a role for the protein in cytoplasmic motility. MAP 1C coelectrophoreses with the beta heavy chain of Chlamydomonas flagellar dynein, and has a sedimentation coefficient of 20S. Exposure to ultraviolet light in the presence of vanadate and ATP results in the production of two large fragments of MAP 1C. These characteristics suggest that MAP 1C may be a cytoplasmic analogue of axonemal dynein. The Rockefeller University Press 1987-09-01 /pmc/articles/PMC2114794/ /pubmed/2958482 Text en 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 Articles
MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties
title MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties
title_full MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties
title_fullStr MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties
title_full_unstemmed MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties
title_short MAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties
title_sort map 1c is a microtubule-activated atpase which translocates microtubules in vitro and has dynein-like properties
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114794/
https://www.ncbi.nlm.nih.gov/pubmed/2958482