The interaction of cystamine with bovine brain tubulin

Asok BANERJEE, Mary Ann JORDAN, Melvyn LITTLE, Richard F. LUDUENA

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Abstract

Microtubule assembly in vitro is sensitive to a variety of non‐physiological sulfhydryl‐oxidizing agents, but the physiological significance of this phenomenon is unknown, since no physiological sulfhydryl‐oxidizing agent has been shown to affect microtubule assembly in vitro. We have accordingly investigated the interaction of tubulin with cystamine. We have found that millimolar concentrations of cystamine inhibit microtubule assembly and induce an abnormal form of tubulin polymerization. Cystamine‐induced polymerization does not occur at cold temperature. Formation of the polymer requires reaction of cystamine with two sulfhydryls which become available at 37°C. In addition, cystamine reacts with about three sulfhydryls at 0°C without inducing polymerization. This latter set of sulfhydryls appear to include one or both of the previously defined βs sulfhydryls whose reaction with N, N'‐ethylene‐bis(iodoacetamide) is markedly inhibited by GTP, maytansine and vinblastine [Roach, M. C. & Luduena, R. F. (1984) J. Biol. Chem. 259, 12063–12071]. Cystamine's specific manner of interacting with tubulin suggests that it may mimic an endogenous sulfhydryl‐directed regulator of microtubule assembly.

Original languageEnglish (US)
Pages (from-to)443-448
Number of pages6
JournalEuropean Journal of Biochemistry
Volume165
Issue number2
DOIs
StatePublished - Jun 1987

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ASJC Scopus subject areas

  • Biochemistry

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