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dc.contributor.authorPaschal, Bryce Mark
dc.contributor.authorShpetner, Howard S.
dc.contributor.authorVallee, Richard B.
dc.date2022-08-11T08:09:02.000
dc.date.accessioned2022-08-23T16:16:23Z
dc.date.available2022-08-23T16:16:23Z
dc.date.issued1987-09-01
dc.date.submitted2008-11-25
dc.identifier.citation<p>J Cell Biol. 1987 Sep;105(3):1273-82.</p>
dc.identifier.issn0021-9525 (Print)
dc.identifier.doi10.1083/jcb.105.3.1273
dc.identifier.pmid2958482
dc.identifier.urihttp://hdl.handle.net/20.500.14038/34317
dc.description.abstractWe 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.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2958482&dopt=Abstract">Link to article in PubMed</a></p>
dc.relation.urlhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2114794/
dc.rights.urihttp://creativecommons.org/licenses/by-sa/4.0/
dc.subjectAdenosine Triphosphatases; Adenosine Triphosphate; Animals; Brain; Cattle; Dynein ATPase; Macromolecular Substances; Microtubule-Associated Proteins; Microtubules; Molecular Weight; Protein Binding
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleMAP 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties
dc.typeJournal Article
dc.source.journaltitleThe Journal of cell biology
dc.source.volume105
dc.source.issue3
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1966&amp;context=gsbs_sp&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/967
dc.identifier.contextkey672259
refterms.dateFOA2022-08-23T16:16:23Z
html.description.abstract<p>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.</p>
dc.identifier.submissionpathgsbs_sp/967
dc.contributor.departmentDepartment of Cell Biology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages1273-82


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