phalloidine and hemiasterlin

phalloidine has been researched along with hemiasterlin* in 1 studies

Other Studies

1 other study(ies) available for phalloidine and hemiasterlin

Article	Year
A missense mutation in Caenorhabditis elegans prohibitin 2 confers an atypical multidrug resistance. Proceedings of the National Academy of Sciences of the United States of America, 2006, Oct-17, Volume: 103, Issue:42 Hemiasterlin is a potent antimitotic peptide that interferes with microtubule dynamics at picomolar concentrations in cell culture. The molecule largely eludes P glycoprotein-mediated drug efflux, and an analog is currently being evaluated in clinical trials as cancer chemotherapy. From a nonclonal genetic screen in Caenorhabditis elegans we isolated eight independent mutants resistant to a synthetic hemiasterlin analog. In one recessive mutant, phb-2(ad2154), a point mutation in prohibitin 2 (E130K) protects worms from drug-induced injury. Data indicate that direct binding of hemiasterlin to prohibitin 2 is unlikely. In fact, C. elegans phb-2(ad2154) was also found to be resistant to numerous other drugs that bind tubulin and to camptothecin, yet this mutant was sensitive to nocodazole and phalloidin. Thus, prohibitin 2 is implicated in a previously uncharacterized pathway of multidrug resistance. Topics: Animals; Antinematodal Agents; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Cell Line; Drug Resistance, Multiple; Genetic Complementation Test; Humans; Molecular Structure; Mutation, Missense; Nocodazole; Oligopeptides; Phalloidine; Prohibitins; Protein Isoforms; Repressor Proteins; Tubulin; Tubulin Modulators	2006

Article

Year

A missense mutation in Caenorhabditis elegans prohibitin 2 confers an atypical multidrug resistance.

Proceedings of the National Academy of Sciences of the United States of America, 2006, Oct-17, Volume: 103, Issue:42

Hemiasterlin is a potent antimitotic peptide that interferes with microtubule dynamics at picomolar concentrations in cell culture. The molecule largely eludes P glycoprotein-mediated drug efflux, and an analog is currently being evaluated in clinical trials as cancer chemotherapy. From a nonclonal genetic screen in Caenorhabditis elegans we isolated eight independent mutants resistant to a synthetic hemiasterlin analog. In one recessive mutant, phb-2(ad2154), a point mutation in prohibitin 2 (E130K) protects worms from drug-induced injury. Data indicate that direct binding of hemiasterlin to prohibitin 2 is unlikely. In fact, C. elegans phb-2(ad2154) was also found to be resistant to numerous other drugs that bind tubulin and to camptothecin, yet this mutant was sensitive to nocodazole and phalloidin. Thus, prohibitin 2 is implicated in a previously uncharacterized pathway of multidrug resistance.

Topics: Animals; Antinematodal Agents; Caenorhabditis elegans; Caenorhabditis elegans Proteins; Cell Line; Drug Resistance, Multiple; Genetic Complementation Test; Humans; Molecular Structure; Mutation, Missense; Nocodazole; Oligopeptides; Phalloidine; Prohibitins; Protein Isoforms; Repressor Proteins; Tubulin; Tubulin Modulators

2006