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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 2004 Sep 17;101(39):14305. doi: 10.1073/pnas.0404506101

Retraction

Samara L Reck-Peterson, Ronald D Vale
PMCID: PMC521152  PMID: 15693149

BIOCHEMISTRY. For the article “Molecular dissection of the roles of nucleotide binding and hydrolysis in dynein's AAA domains in Saccharomyces cerevisiae,” by Samara L. Reck-Peterson and Ronald D. Vale, which appeared in issue 6, February 10, 2004, of Proc. Natl. Acad. Sci. USA (101, 1491–1495; first published January 30, 2004; 10.1073/pnas.2637011100), the undersigned authors wish to note the following: “In conjunction with a follow-up project regarding these mutations, we resequenced several of the mutant yeast strains and found that the genes in two of the eight analyzed mutant strains (the E2488Q mutation in the AAA3 domain and the K2766A mutation in the AAA4 domain) no longer contained the mutation and instead were wild type. The correct K2766A mutation does not have a defect in either nuclear segregation or microtubule dissociation as originally reported; however, there is a modest defect (∼50% decrease) in microtubule binding. More significantly, the true E2488Q mutation demonstrated a severe nuclear segregation phenotype and a defect in the release of dynein from microtubules with ATP, comparable to that reported for the nuclear hydrolysis mutation in AAA1. Thus, our initial conclusion that the AAA site 3 ATP hydrolysis mutation has no phenotype is incorrect. We now know that ATP hydrolysis in both AAA1 and AAA3 is essential for dynein function and that nucleotide binding at AAA2 and AAA4 is necessary for maximal levels of microtubule binding in vitro.”


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